K C Chandran Nambiar
Sulphur has a dominant position in homoeopathic materia medica, and is probably one of the the most prescribed drugs in homeopathic practice. Sulphur has been symbolically entitled as the ‘king of antisorics’ by our great masters. It is well proven, and it represents the richest symptomatology in our whole materia medica. Some homeopaths as a routine manner administer a dose of sulphur in high potency at the termination of treatment for acute diseases, and also at the beginning of treatment for chronic diseases. There is also a wide-spread practice of administering a dose of sulphur in high potency when other ‘seemingly well indicated’ remedies fail, so as to arouse reaction. There is also a saying that the frequency of prescibing sulphur and practitioner’s knowledge of materia medica have an inversely proportional relationship, which means, the less the doctor knows his materia medica, the more he is compelled to use sulphur frequently in his practice. Even though one may basically differ regarding the acceptability of such concepts and practices, they ultimately indicate the paramount importance accorded to sulphur in homoeopathy.
As part of a logical continuation of the scientific interpretation of ‘Similia Similibus Curentur’ and ‘Potentization’ discussed in my article “Dialectical Homoeopathy’, I think it would be appropriate to delve into a deeper analysis of the diverse roles sulphur plays in various biological processes in the organism. It may necessarily lead to the study of the various molecular blocks and biochemical deviations underlying the vast symptomatology of suphur. Such an analysis may also show the way for similar scientific studies about other important drugs of homoeopathic materia medica, which will especially be relevant when we try to present homoeopathy as a higher branch of modern molecular medicine.
In my opinion, we have to undertake a huge reasearch project to study the symptomatology of all important drugs of our materia medica, in such a way that we can identify their individual symptom complexes in relation with the structure and configuration of the active groups of various constituent molecules of the drug substances. As in the case of every state of pathology, no drug symptom can be produced in an organism without a corresponding chain of molecular processes underlying it, initiated by the interaction of some or other drug molecules with some or other biological molecules. From a scientific point of view, drug symptoms should be interpreted and utilized as minute biological indicators of corresponding molecular blocks and biochemic deviations brought about in the organism by the action of drug molecules. We should begin learning materia medica from this scientific perspective, at least in future.
To begin with, let us take up the study of sulphur. For this, we have to collect and analyze all the available information regarding the diverse biochemical processes in the organism in which sulphur has a role to play. Obviously, such a study includes not only the study of various natural biological molecules in the organism, but also various exogenic and endogenic pathogenic molecules containing sulphur, and the nature and type of molecular inhibitions caused by them.
According to Samuel Hahnemann, the ‘miasm’ of ‘psora’ is the main cause of chronic diseases. As per his interpretation, ‘psora’ is ‘suppressed itch’, which means, the chronic constitutional susceptibility to diseases, resulting from the suppression of ‘itch’ appearing on the surface of the skin. Homeopathic theory of ‘chronic diseases’ is built up on this fundamental concept of ‘psora’. He describes ‘psora’ as a hiding ‘multi-headed hydra’, which expresses its presence in the organism in the form of multitudes of chronic ailments with periodical acute exacerbations, persisting until death. Potentized sulphur is supposed to be a an antidote of this chronic miasm of ‘psora’, and hence the saying “ sulphur is the king of anti-psorics”.
It is interesting to observe at this point that toxins released by bacteria found in lesions of ‘itch’, are complex chemical molecules of protein nature, containing ‘sulphide’ radicals in their active groups. The presence of sulphur-containing amino acid ‘cysteine’ in the bacterial proteins is responsible for this factor. During infection, bacterial toxins bind to various biological molecules in the organism using this ‘sulphide’ group as the ligand. Antibodies are formed in the organism by a process of ‘molecular imprinting’ of certain class of protein molecules called globulins, with these bacterial toxins. Obviously, the antibodies are molecular imprints of these bacterial toxins, and contain three-dimensional complementary configurations of this ‘sulphide’ group on them. These molecular imprints can immunize the organism against further infections, by acting as neutralizing agents towards the bacterial molecules, and hence the name ‘antibodies’. At the same time, these anti-bodies or molecular imprints can create unwanted molecular blocks in diverse biochemic channels in the organism, by binding themselves to various sulphide-containing bio-molecules, due to their configurational affinity towards sulphide groups.
These molecular blocks and biochemical inhibitions arising therefrom are the real cause of chronic diseases that Hahnemann attributes to ‘miasm of ‘psora’. We already know that the antibodies produced against bacterial skin infections or ‘itch’ may attack heart, kidney, brain, and other vital organs causing different types of diseases. Streptococcal and staphylococcal antibodies formed against acute throat and teeth infections may attack synovial membranes of joints, endocardial linings, and valvular structures of heart. During drug proving, sulphur also binds to the same molecular targets as the bacterial toxins, and produces similar molecular deviations and similar symptoms. The similarity between certain symptom groups produced by these bacterial infections and the homeopathic provings of sulphur correlates with this observation. Potentized sulphur, being molecular imprints of sulphur molecules in alcohol-water medium, can act in the same way as ‘itch’ antibodies. Here we get the scientific explanation for the observation of Hahnemann that potentised sulphur is the most important antipsoric medicine, ‘The King of Antipsorics’. During drug proving, ionized sulphur may also compete with sulphide radicals of various biological protein molecules, thereby preventing their normal biochemical interactions.
It is already known that the amino acid called ‘cysteine’, containing ‘sulphide’ groups, play an important role in almost all molecular interactions in the organism, especially involving protein molecules of enzymatic functions. This may be the reason for the appearance of so many symptom groups, involving almost every biochemical channels of the body, in the homoeopathic proving of sulphur. Potentized sulphur, being molecular imprints with three-dimensional complementary configuration of sulphur, can neutralize the sulphide groups of bacterial toxins, by binding to them. More over, molecular imprints of sulphur can compete with the bacterial antibodies, in their interactions with biological molecules, and act as a most powerful ‘anti psoric’ drug. As crude drugs also, sulphur exhibits an anti bacterial and antifungal action, by the competitive relationship of sulphur ions with sulphide groups of such proeins.
A few words about the homeopathic nosodes such as ‘psorinum’,
‘tuberculinum’, ‘streptococcin’, etc. will be relevant here. These nosodes in the potentized form contain molecular imprints of antibodies themselves, formed in the organism against bacterial toxins. Hence, these potentized nosodes will be more useful in treating the chronic miasmatic effects of itch and other bacterial infections, whereas potentized suphur will be appropriate to deal with the direct bacterial infections and bacterial toxins themselves. Hahnnemann also has observed that potentized ‘psorinum’ is more appropriate antipsoric in the treatment of chronic diseases, where as potentized ‘sulphur’ will be ideal for acute complaints of ‘psora’.
Sulphur in Biological System
Sulphur is an essential element for the existence of life. It is an indispensable part of various aminoacids, proteins, enzymes and co–enzymes. Sulphur is a constituent of many important bio-molecules such as cysteine, methionine, coenzyme-A, iron-sulphur clusters, biotin, lipoic acid, molybdopterin, ERNA, thio-nucleiosides, and thiamine. These molecules are participants in various vital biochemic processes including the synthesis of proteins.
Sulphur is also very important in the metabolism of pathogenic organisms such as virus, fungi and bacteria, and as such, play in major role in causing various ailments in human organism. We know, bacteria belonging to mycobacterium group are responsible for disease such as tuberculosis and leprosy. Studies regarding metabolism of these mycobacteria have greately enhanced our understanding about the role of sulphur in the molecular mechanism of such diseases. Many studies have already taken place regarding sulphur-containing molecules discharged by bacteria belonging to ‘treponema denticola’ group. This bacteria are widely seen associated with teeth and gum diseases of human beings. Several toxic molecules let out by fungi contain sulphur. All these facts make it very clear to us why sulphur adorns such a prominent place in homeopathy. We should understand how such chemical molecules produce diseases in men and how medicines act against them.
Sulphur is an indispensable constituent in the biochemical processes of plant kingdom also. The sulphur-containing phyto-chemical molecules synthesized by plants, such as glutathione, sulpholipids, alliins, glucosinolates and phytochelates enable them to defend themselves against insects and over come environmental stress. We use these phytochemicals as powerful therapeutic agents also.
Sulphur acts as the bridging ligand of the important enzyme which controls the use of oxygen in the living cells, known as cytochrome C-oxidase. This indicates the crucial role of sulphur in the very existence of life itself. Certain bacteria maintain their life itself by depending on sulphur compounds. It is the hydrogen sulphide excreted by such bacteria inhabiting our body which imparts the offensive odour to our sweat and excretions. The peculiar smell produced when organic materials get degenerated is also due to the presence of sulphur in them.
Sulphur is contained in various defence molecules synthesized by bacteria. All the antibiotics synthesized by bacteria such as pencillins, cephlosporins, monobactams and their synthetic derivatives contain sulphur.
There is a lot of sulphur contained in the horns, nails, hair, skin and other appendages of animals. Their charecteristic hardness is due to the strong ‘disulphide’ bonds formed between their protein molecules.
‘Sulfhydryl(thiol)’ groups containing sulphur play a very important role in the biochemical processes of all living organisms. Thioredoxins containing ‘thiol’ groups are indispensable in the synthesis of various biological molecules.
‘Thiol’ contained in coenzyme-A participate in the oxidiation activities of pyruvate-fatty acid which is the integral part of the energy metabolism in the cells. Thiol groups of glutathione and mycothiol protect the cells by deactivating dangerous oxidants. Sulphur is also a factor in the structure of many messenger molecules also.
Sulphur ions are comparatively much larger than similar ions. More over, their peculiar electron distribution and ability for easy polarization make them powerful nuceleophiles. It is because of tese peculiarities that Sulphur has attained so much importance in the biochemical processes.
Proteins and Sulphur
Among the twenty amino acids essential for the synthesis of proteins, only cysteine and methionone contain sulphur. Only if we get a correct understanding about these two amino acids including their structure and the role they play in organic processes, will we be able to explain the biological importance of the suplhur.
H3C-S-(CH2) 2-CH-COOH HS-CH2-CH-COOH
The amino acid ‘cysteine’ has to be particularly subjected to our study. Its ‘R’ group is an ‘HS’, containing sulphur. A peculiarity of ‘HS’ is that they can form mutual disulphide bonds. Such groups are called ‘thiol’ groups or ‘sulphydryl’ groups.
‘HS’ or ‘thiol’ is the functional group of the amino acid called ‘cysteine’. This thiol group has great importance in various bio-chemical processes. If ‘cysteine’ residues contained in different protein molecules or in different parts of the same molecule happens to come into contact with each other, the HS groups in them interact with each other by oxidization process and become ‘cystine’ through disulphide bonding(S-S). This process plays a very important role in the formation of the highly complex three-dimensional tertiary structure of protein molecules. Multi-unit proteins are also formed by this way.
These ‘disulphide bonds’ are crucial in the structure of several antibodies. Antibodies bind to the antigens by ‘thiol’ groups contained in the cysteine residues at their active sites. Thiol groups of cysteine residues contained in the active sites of enzymes help substrates to remain bound with enzymes and enable the smooth conduct of biochemical transformations. Cysteine residues at the active sites of enzymes belonging to the group of ‘cysteine proteases’ may be cited as examples. The importance of ‘HS’ groups of the amino acid ‘cysteine’ in various enzymatic interactions has to be clearly understood.
The phenomenon of curling found in hair is due to disulphide bonds formed between cystenie residues. The chemicals used for curling and straightening of hair work by the oxidization-antioxidation processes of cysteine residues contained in the hair.
The HS groups contained in the cysteine residues are capable of reacting with the ions of heavy metals ( Pb, Hg, Ag). Such reactions will make proteins inactive by effecting deformities in their three dimensional structure. This is the molecular mechanism behind heavy metal poisoning. Sulphur ions are capable of weakening the reactive power of metal ions by binding themselves on them. This happens in the case of metaloenzymes where metal ions function as co–factors. Thiol groups in cysteine are easily subjected to oxidization. Their reactive efficiency is tremendously enhanced when ionized. Because of this peculiarity, ‘thiol’ groups become participants in many biochemical processes.
Insulin is rendered inactive in certain circumtances due to the presence of cysteine. It is possible for cysteine to inactivate the three disulphide bonds contained in insulin molecules by deoxidizing and changing their structure, In the conditions of hypoglycema where in the sugar content of blood is alarmingly reduced, cysteine is employed as a drug to make insulin inactive. Apart from cysteine , thiamine and vitamin C are also used for this purpose. Here it is evident why health supplements containing cysteine should not be given to diabetic patients. It is to be specially mentioned that foreign molecules containing sulphur are capable of intervening in the biochemical processes connected with insulin.
The disulphide bonds formed between cysteine residues are responsible for the phenomenon of cross linking between protein molecules. This type of cross linking has great importance in placing molecules like insulin un impaired at their appointed positions.
Glutathione which is formed through the combination of amino acids like cysteine, glycine and glutamic acid is an important antioxidant in the body. Thiol groups and sulphur which is a part of it play an important role in the synthesis and functioning of glutathione.
Dissulphide bonds play an import role in the post-translational modifications of proteins. It is through disulphide bonds between cysteine residues that the peculiarl three dimensional shapes and foldings of proteins molecules working in extracellular medium are shaped. In case such bonds are not formed protein molecules become deformed and incapable of performing their biochemical functions.
The metal ions such as zinc, iron, copper, nickel etc which function as co-factors of several enzyme systems actually connect with appropriate enzymes through thiol groups contained in their cysteine residues. Example are: zinc in alcohol dehydrogenase, iorn in cytochrome P450, nickel in [NiFe]-hydrogenases and copper in blue-copper proteins.
It is with the help of enzymes known as protein disulphide isomerases that the S-S disulphide bonds in proteins are formed. It is possible for various chemical molecules containing sulphur to bind themselves competitively on these enzymes and inhibit their functions. It can be legitimately considered that many symptoms observed in homoeopathic proving of sulphur and sulphur-containing drugs indicate these molecular inhibitions.
Cysteine residue is contained in the active sites of many enzymes. Sulphur(thiol) groups contained in the enzymes play a crucial role in enzymatic interactions. Antibodies also interacts with other molecules through their thiol groups. Molecular mechanism of immune disorders also should be understood in this perspective.
Cystathionine gamma-lyase and cystathionine beta-synthase, are two important enzymes involved in the synthesis of cysteine. Sulphur ions and sulphur-containing drugs may be capable of inhibiting these enzymes through competitive molecular blocks.
Thiol groups are contained in the molecules of various phytochemicals. Various viral, bacterial and fungal toxins also contain thiols. Such chemicals can interfere in the molecular interactions of proteins in the organism resulting in multitudes of pathological conditions. Symptomatology of homeopathic provings of those drugs should be subjected to a re-reading with this scientific perspective.
Different types of active groups containing sulphur, like Sulfonyl, Sulfo Sulfinyl, Sulfhydry(Thiol) Thiocynate and Disulphide are capable of interveining in biochemical processes.
Immunoglobulins or antibodies represent a very important class of proteins, playing crucial roles in the biological system. They are found in blood, lymph and other body fluids. These antibodies are part of immune system of the organism. These antibodies are synthesized in plasma cells known as lymphocytes. Antibodies are molecules belonging to globulin proteins. Mainly there are five type of immunoglobulins. Antigens are bound to antibodies using their active groups known as epitopes. The site of binding on antibodies are known as peritopes.
The molecular components of an immunoglobin are four polypeptide chains bound by disulphide bonds. These disulphide bonds are formed by thiol groups of the cysteine residues contained in them. It is in the presence of an enzymes known as protein disulphide isomerase PDI that the formation and breaking of these bonds take place. Moreover, this enzyme participate in many ways in the antigen-antibody process. Involvement of this enzyme is necessary in binding antigens with the molecules of major histocompatability complex(MHC1) which is very important in the defence system of the organism.
Sulphur ions and foreign molecules containing sulphur are capable of competitively binding on disulphide isomerase(PDI) and make them inactive. This is the molecular mechanism of medicinal materials containing sulphur adversely affecting the immunity.
Peritomes of antibodies are subjected to molecular imprinting with epitome groups of antigens. The antibodies thus imprinted have special affinity to the concerned antigens, due to the complementary configurations created by imprinting. It is because of this special complemetary affinity that antibodies are able to recognize exact antigens. It has been proved that these antibodies maintain affinity not only with imprinted antigen epitoms but also with other molecules having similarity in shape with them. Because of this, the antibodies misunderstand the molecules essential for the body as antigens and create different types of molecular blocks by binding on them. This phenomenon gives the chance for different type immune related diseases. A detailed discussion of this matter has already been made else where in the same article where miasm is discussed. The potentised homoeo preparations have proved to be capable of cradicating such conditions of illness.
Many bacterial viral toxins act as antigens. The groups of symptoms appearing in many diseases due to such bacterial infections exhibit similarity with homoeopathic provings of sulphur. The reason for this is evident. We used to treat effectively such conditions of illness using high potency sulphur on the basis of Similia Similibus Curentur.
Biotin is a vitamin containing sulphur. Biotin is the co–factor which makes active several important enzymes like, Acetyl-CoA carboxylase, Pyruvate carboxylase, Methylcrotonyl-CoA carboxylase, Propionyl-CoA carboxylase. Many foreign molecules containing sulphur groups compete with biotin in interacting with the above mentioned enzymes and this subject them to competetive inhibitions. Certain bacterial and viral toxins also function in the same manner. As a result a condition equivilant to the absence of biotin is created and condition of illness similar to that is produced. This will adversely affect the natural growth of cells, and the metabolism of lipids and amino acids. Falling of hair, falling of eyebrow, greying, disinterest in food, eczema, dermatils, drying of skin, increase in blood sugar, numbness of hands and legs, many types of bacterial infections, fungus infections, mental problems and deterioration of immunity etc. result.
Ubiquitins are regulatory protein molecules containing lysine residues playing a very important role in various biochemical processes. By binding themselves on different types of protein molecules ubiqiutins ensure the configurational stability of proteins, and empower them to do their stipulated chemical functions. Ubiqiutin polypeptides also act as markers of protein molecules, preparing them for their calabolism. Ubiquitin-activating enzyme E1, ubiquitin-conjugating enzyme E2, ubiquitin-protein ligases E3 etc are the enzymes associated with ubiquitin interactions.
The first stage of this process known as ubiqiutination is performed with the help of cysteine residues positioned at the active sites of the ubiqiutine-activating enzyme E1. Molecules containing active groups of sulphur are capable of competitively binding on these enzymes and making them inactive. This phenomenon underlies many types of disease we face today.
Ubiqiutination is crucial in many organic processes like antigen processing, apoptosis, biogenesis of organelles, cell cycle and division, DNA transcription and repair, differentiation and development, immune response and inflammation, neural and muscular degeneration, morphogenesis of neural networks, modulation of cell surface receptors, ion channels and the secretory pathway, response to stress and extracellular modulators, ribosome biogenesis, viral infections etc. The plentifulness of diseases conditions likely to be caused by obstructions to the above mentioned organic processes is very evident. All these factors are to be taken in to account when we make a study of the homeopathic symptomatology of Sulphur.
Tyrosine sulfation is the process in which sulfate groups are added to tyrosine residues of proteins synthesized in the cells. This chemical process take place in golgi apparatus. In this process, sulphate ions are extracted from Adenosine 3′-phosphate 5′-phosphosulfate (PAPS) and added to tyrosine residues of proteins, with the help of an enzyme known as Tyrosylprotein sulfotransferase (TPST). Exogenous sulfate ions are capable of creating molecular blocks in these enzymes, through competitive relationship. Tyrosine sulfation is essential for the molecular interaction of proteins. Many proteins such as adhesion molecules, G-protein-coupled receptors, coagulation factors, serine protease inhibitors, extracellular matrix proteins, and hormones are subjected to tyrosine sulfation.
The studies dealing with the chemical process known as tyrosine sulfation and its partipant enzyme systems are even now incomplete. The influence they exert in the processes like the growth of hair, regulating body weight and reproduction is almost fully uncovered. By this time it has been made very clear that the sulfation of protein is an important area of biochemical activities. We have to constantly follow the scientific researchs taking place in this area positioning ourselves in the perspective of Homoeopathy. It will be very interesting to learn the crucial role the sulphate ions play in the organic system.
Glucosinolates are a class of chemical molecules containing sulphur and nitrogen, found naturally in plants,. They are used as medicinal drugs and natural pesticides. Glucosinolates are abundant in mustard, radish, horse radish, maca, cress, cabbage, brussels sprouts, kohlrabi, kale, cauliflower, broccoli, turnip, swede(rutabaga) and rapeseed.
Sinigrin (allylglucosinolate or 2-propenylglucosinlate) is a glucosinolate found in plants like broccoli belonging to the brassica family. It has been proved that sinigrin is capable of preventing the multiplication of cancer cells. Sinalbin, another glucosinolate found in mustard also belong to the same group. These are converted to allyl isothiocyanate by the action of certain enzymes.
It has been observed that the organo-sulphur compound sulforaphane , contained in certain plants can be used as curative agent against helicobacter pylori bacteria, the causative agent of gastric ulcers. Sulforaphane is also found to be useful as external application to protect skin from ultra violet rays.
Thiocyanate ions containing sulphur inhibit the production of thyroide hormones like thyroxine and triiodothyronine. This is because they are capable of producing molecular blocks by competing with iodine. The thioglycoside such as alliin contained in garlic are chemically sulfoxides. This function both as antioxidant and hydroxyl radical scavenger, because of the presence sulphur ions in them. It has been proved in the laboratory tests that the functional ability of phagocytes in blood is increased in the presence of alliin.
Lenthionine is the organo-sulphur compound contained in certain types of fungi. These sulphur –containing molecules prevent the clotting of blood. Certain organo-sulphur compounds contained in grlic also function in the same manner. These molecules inhibits the enzymes called C-S lyase.
Thiamine is included in the group of B-complex vitamins. It is a chemical compound containing sulphur. Thiamine diphosphate (ThDP), which is the active form of thiamine works as a co–enzyme in various enzymes systems which regulate catabolic processes of amino acids and sugars. Thiamine is synthesized in bacteria, fungi and plants. Thiamine required by animals has to be obtained through food. In its absence may cause the disease called beriberi, affecting the nervous system and circulatory system. General debility, emaciation and mental disorders are also observed.
Thiamine (C12H17N4OS) is a vitamin soluble in water. Sulfites are capable of inhbiting thiamine. Thiaminase enzymes contained shell fishes and certain other fishes, Hydroxyphenols such as Caffeic acid, Chlorogenic acid, Tannic acid foud in plants also make thiamine inactive. Glycocides like quercetin and rutin also deactivate thiamine in the same manner.
Enzymes like phosphatase, pyrophosphatase, thiamine pyrophosphokinase, Na+-dependent ATPase also adversely affect the availability of Thiamine.
Following are the biochemically active forms of thiamine: thiamine monophosphate(ThMP), thiamine diphosphate(ThDP), thiamine triphosphate (ThTP), adenosine thiamine triphosphate (AthTP), adenosine thiamine diphosphate (AthDP). Thiamine in the form of Thiamine diphosphate (ThDp) act as co–factors for enzymes such as pyruvate dehydrogenase, 2-oxoglutarate dehydrogenase , branched-chain α-keto acid dehydrogenase, 2-hydroxyphytanoyl-CoA lyase and transketolase, which play major roles in carbohydrate metabolism.
The enzyme named transketolase, which requires thiamine as co-factor, participates in the synthesis of sugars such as deoxyribose, ribose and NADPH. Pyruvate dehydrogenase(PDH), and 2-oxoglutarate dehydrogenase(OGDH), both having thiamine as co-factors, are participants in synthesis of ATP. These enzymes are also important in citric acid cycle, and synthesis of myelin and acetylcholine.
The deficiency of thiamine cause a disease called peripheral neuropathy. This adversely affects sensory, motor and reflex activities in the limbs. Mental problems, emaciation and cardiac dysfuntions also are very serious problems in children. Excessive consumption of alcohol may result in deficiency of thiamine. The symptoms of serious thiamine deficiency are found in HIV-AIDS patients. Understanding the molecular mechanism of symptoms of thiamine deficiency exhibiting in HIV infection may help in developing an effective homoeopathic treatment protocol for such diseases.
Werenicke’s encephlopathy is a rare disease caused by the severe deficiency of thiamine. Its symptoms are decrease in the motility of eyes, unsteadiness, and mental disorders. Koresakott psychosis is a more aggravated form of the same disease.
Genetic disorders such as thiamine responsive megaloblastic anemia, Leigh disease (subacute necrotizing encephalomyelopathy, opsoclonic cerebellopathy (a paraneoplastic syndrome), Nigerian seasonal ataxia etc. are associated with thiamine deficiencies. Sulphur ions are capable of creating molecular blocks in the enzymes involved in thiamine metabolism. Compounds containing sulphur or sulphites are directly capable of rendering thiamine molecules inactive.
Iron – Sulphur Proteins:
These are the proteins containing iron–sulphur clusters. Enzymes such as NADH dehydrogenase, hydrogenases, coenzyme Q- Cytochrome C reductase, succinate-coenzyme Q reductase, nitrogenase and metalloproteins such as ferredoxins are exmples. The sulphur necessary for making of lipoic acid and biotin is made available from iron–sulphur clusters. They play their vital roles in the oxidization and antioxidization processes in mitochondria. Their presence is essential in oxidative phosphorylation processes as well. Nitric oxide is capable of rendering iron–sulphur proteins inactive.
The active group of iron-sulphur proteins are cysteine residues containing ‘thiol’ group. It is specially noteworthy that sulphur ions and exogenous molecules containing sulphur groups are capable of competitive intervention in biochemical processes related to iron-sulphur proteins.
Sulphite oxidase is an important metalo-enzyme found in the mitocondria of animals. This enzyme is very crucial in the process of ATP synthesis. Molybdopterin molecules containing molybdinum acts as co–factors for this enzyme. This co–factor is bound to the sulphur of cysteine residues in the enzyme molecule.
Exogenic sulphur ions, suphur-containing drugs and bacterial-viral molecules are capable of competitively binding on the molybdopterin molecules, thereby preventing them from connecting with the enzyme molecules. In the absence of the appropriate co-factor, the enzyme is unable to execute its biochemic functions, leading to a condition of pathology amounting to absence of sulphite oxydase. Neurological disorders, mental retardation, physical deformities and brain disorders are the result. It might even result in death. In some cases, absence of this enzyme may happen due to defects in genetic expression also. Any how, we have to bear in mind the role of sulphur in sulphite oxidase metabolism, while engaging in a scientific study of sulphur symptomatology.
Co-factors are indispensible components of several important enzyme systems. Lipoic acid function as such a co–factor. It is an organo-sulphur compound containing sulphur in its active group, which is a disulpide. These exist in the cells in the form of dihydrolipoic acid. Often it is not found in the organism in independent form, but as part of various enzyme comlplexes like pyruvate dehydrogenase complex, glycine cleavage gomplexes etc .
Lipoic acid is a food antioxidant as well. It is capable of reviving glutathione, vitamin C and vitamin E. It functions as a good molecular scavenger due to the presence of disulphide groups in it.
It has been already proved that sulphur ions and various drug molecules containing sulphur are capable of inhibiting certain enzyme systems associated with lipoic acid synthesis, thereby negatively affecting the availabilty of lipoic acid in the organism. This point has to be especially considered in our scientific study of symptomatology of sulphur. More over, sulphur ions and sulphur-containing drugs may compete with lipoic acid in binding with their molecular targets, including the enzyme systems. Obiously, some of the symptoms of sulphur proving may be representing the pathologic conditions arising from such lipoic acid deficiency.
Leprosy is a disease caused by the bacteria known as mycobacterium leprae. Dapsone (diamino-diphenyl sulfone) is widely used for the treatment of leprosy. Dapsone interferes in the biochemical processes through its active groups containing sulphur(sulfone). Antibiotics belonging to sulfonamide group also work through the same mechanism. Dapsone effects its therapeutic properties against leprosy by interfering in the synthesis of dihydrofolic acid which is essential for the metabolism of these bacteria.
Apart from leprosy, dapsone is found effective in many disease like pemphigoids, dermatitis herpetiformis, linear immunoglobulinA dermatosis, lichen planus, acne etc. Sulphone group of dapsone compete with sulphur-containing proteins of infectious agents in binding with native biological molecules, thereby exhibiting their terapeutic effects. It is interesting to note that we can see many groups of symptoms of above said diseases in the homeopathic symptomatology of sulphur. It has been also found that dapsone can be used in the treatment of diseases like pneumocystic pneumonia (PCP), idiopathic thrombocytopenic purpura, and toxoplasmosis. Daspone has been indicated as an antidote for some kinds spider poisons also. Dapsone has been effectively used as external application in some non- bacterial skin diseases also.
It has also been observed that the use of dapsone results in many types of side effects such as hemolysis, hemolytic anemia, methemoglobinemia, agranulocytosis, aplastic anaemia, cholestatic jaundice, toxic hepatitis, nausea, headache, skin rashes, eosinophilia, insomnia, psychosis, peripheral neuropathy etc. It has been proved that dapsone is capable of interfering in the enzyme system known as cytochrome P450. Since dapsone is a drug containing sulphur in its active group, these observations are relevant in the study of biological roles of sulphur.
Further studies required
Sulphur plays many more important roles in biological processes than those already discussed above. Here we have considered some prominent examples only. Homoeopathic provings and symptomatology of sulphur have to be subjected to a thorough re-reading in the light of latest available knowledge regarding the diverse biochemical processes sulphur participates in the living organism. Such a scientific re-reading might help us identify the exact molecular errors underlying each group of complex subjective and objective symptoms attributed to the homeopathic provings of sulphur.
Various sulphur-containing drugs of plant, mineral or animal origin, bacterial and viral products, and new generation sulphur-containing synthetic drug molecules also have to be subjected to in-depth study of their chemical structure, biochemical involvement and symptomatology. Such a scientific study may enable us to understand how constitutions of sulphur get evolved in idividuals, as a cumulative result of genetic factors, environment and life style, including food, drinks, bacterial or viral diseases and usage of medicinal substances. A comparative study of symptomatology of sulphur with other drugs containing sulphur like natrum sulph, hepar sulph, kali sulph, ars sulph, aethiops, cadmium sulph, calc sulph, carboneam sulph, chininum sulph, ferrum sulph, hydrast sulph, mag sulph, manganum sulph, merc suph, sulph Iod, scid sulph and zinc sulph, petroleum etc., will be much interesting and useful. All the similar symptom groups found in the symptomatologies of all these substances can be attributed to the suphur content in these drugs.
We have already seen that various viral and bacterial toxins contain sulphur. Suplhur is present in most of the food articles we consume. The same is the case with the drugs used by different medical systems in the treatment of diseases. Sulphur ions, sulphur-containing drugs and sulphur- containing bacterial and viral toxins can compete with the thiol groups of various protein molecules in our body such as enzymes and antibodies, in binding with their legitimate molecular targets, resulting in unwanted molecular blocks and pathologic conditions. All these factors may contribute in building up constitutional states of sulphur in a large percentage of population, by creating diverse types of biochemic deviations in their organism. This indicates the real depth and gravity of the ‘miasm’ which Hannemaan called ‘psora’ in the whole human race. This study clearly shows how much important is the use of potentized sulphur as a constitutional medication for the protection of our health and vitality.
Homeopathy, based on the principle of ‘Similia Similibus Curentur’ uses potentized drugs, containing molecular imprints or ‘hydrosomes’ of drug molecules. Obviously, sulphur, which plays versatile roles in normal physiology and various states of pathology, will be the most important drug in potentized form in homeopathic therapeutics. As such, the title ‘the king of antipsorics’ is not at all an exaggerated statement as far as sulphur is concerned.
K C Chandran Nambiar
Author of: DIALECTICAL HOMEOPAHY
Developer of: SIMILIMUM ULTRA Homeopathic Software
Email: email@example.com . Mobile: 91 9446520252