568 South African Journal of Science 98, November/December 2002
The link between vitamin B12 and
methylmercury: a review
S.M. Chemaly
The mercuric ion (Hg2+) is methylated in the sediment of aquatic
systems to give methylmercury (CH3Hg+), which is bioaccumulated
in fish and has high toxicity for humans. Methylcobalamin, the
methyl derivative of vitamin B12 and a coenzyme in enzymatic
methyl transfer, is able to methylate mercury(II). In the chemical
reaction, the mercuric ion acts as an electrophile towards methyl-
cobalamin in aqueous solution, giving aquocobalamin and methyl-
mercury. It has been shown that sulphate-reducing bacteria,
Desulphovibrio desulfuricans, methylate mercury(II) in aquatic sed-
iments and that they use methylcobalamin to methylate mercuric
ion. The methylation of mercury may be promoted by a synergistic
interaction between sulphate-reducing bacteria and methanogens.
Mercury and methylmercury
Mercury is poisonous in all its forms: as mercury vapour from
metallic mercury, inorganic mercury and especially organic mer-
cury. The three major species of mercury that are toxic to human
beings are metallic mercury, Hg(0); inorganic mercury in oxida-
tion state Hg(II); and organic mercury, in particular methyl-
mercury. The effects of mercury on the health of humans
depend on the particular species of mercury and the route by
which it is absorbed. Metallic mercury is absorbed mainly via the
lungs and the skin and causes damage to the lungs and the brain.
Inorganic mercury(II) is taken up via intestinal absorption from
contaminated food or water and gives rise to corrosion of the
intestinal tract and kidney failure. Organic methylmercury is
also taken up via intestinal absorption and causes damage to the
brain and the developing foetus. Both mercury(II) and methyl-
mercury are soft acids (large and polarizable metal ions) and
bond well with soft bases, such as the sulphydryl groups of
cysteine residues in proteins. Methylmercury is more toxic than
mercury(II).1 The reason that methylmercury is so toxic for
humans is that it is lipophilic and is thus able to pass through the
blood–brain barrier. The methylmercury then reacts with
sulphydryl groups in proteins in the brain, causing irreversible
damage to cells of the central nervous system.2 Methylmercury
can also cross the placental barrier and this leads to accumula-
tion in the foetus.3
Mercury is the only metal that is a liquid at room temperature.
Inorganic mercury exists as mercury(I) and mercury(II). Mer-
cury(I) is almost insoluble in aqueous solution. Mercury(I) is a
dimeric species, Hg22+, with a strong Hg–Hg bond. In aqueous
solution, Hg22+ undergoes disproportionation to give metallic
mercury (Hg0) and the mercuric ion (Hg2+), both of which are
highly toxic. The mercuric ion is very much more soluble in
aqueous solution than the mercurous ion. The mercuric ion can
be methylated to give methylmercury (CH3Hg+), which is 50 to
100 times more toxic than the mercuric ion.4 The conversion of
mercuric ion to methylmercury occurs in the sediment of aquatic
*Department of Pharmacy and Pharmacology, University of the Witwatersrand Medical
School, 7 York Road, Parktown 2193, South Africa. E-mail: chemalysm@therapy.wits.ac.za
Review Articles
systems4,5 and the methylmercury diffuses into the water.
Methylmercury reacts with sulphide ion, S2–, (from H2S pro-
duced by microbes) to give dimethylmercury, (CH3)2Hg, and
mercuric sulphide, HgS. Hg2+ is also converted to HgS by H2S.
Mercuric sulphide is poorly soluble in water and provides a
means of removing mercury(II) from solution and of preventing
the methylation of mercury(II).1,3
The interconversions between mercury species in sediment
are given below:
methylation
Hg22+ → Hg(0) + Hg2+ → CH3Hg+
↓S2–
HgS
2CH3Hg+ + S2– → (CH3)2Hg + HgS
Methylation of mercury takes place under both aerobic and
anaerobic conditions but occurs much more rapidly under
anaerobic conditions. The pH of the medium is important for the
methylation of mercury — CH3Hg+ is more stable under neutral
to acid conditions but (CH3)2Hg is more stable under basic condi-
tions. The rate of production of CH3Hg+ is raised by increasing
salinity of water.1
Methylmercury is a major pollutant of aquatic systems and is
bioaccumulated in fish and shellfish. Up to 1.5% of the total
mercury in sediments and about 2% of the mercury in seawater
exists as methylmercury but about 80% of the total mercury in
fish is methylmercury.1 Fish appear to have a low rate of elimina-
tion of methylmercury and the amount of methylmercury in fish
increases with age and size; the methylmercury does not appear
to harm the fish.3 The Minamata and Niigata disasters in Japan
were caused by the eating of fish contaminated by methyl-
mercury.4
Methylcobalamin and related methylcorrinoids
Methylcobalamin, which is the methyl derivative of vitamin
B12, was first proposed as the methylating agent for mercury by
Wood and coworkers6 and independently by Jensen and
Jernelöv,7 both in 1968.
The structures of vitamin B12 (cyanocobalamin) and methyl-
cobalamin are given in Fig. 1. Cobalamins contain a central
cobalt atom in the Co(III) oxidation state and are six-coordinate.
The cobalt is coordinated by five nitrogen atoms, four from the
delocalized corrin ring (in the equatorial plane) and one from
the 5,6-dimethylbenzimidazole base, which is connected via a
nucleotide side-chain to the corrin ring. The sixth coordination
position is occupied by CN in vitamin B12 (cyanocobalamin) and
CH3 in methylcobalamin. Methylcobalamin contains a Co–C
F-bond. The Co(III) cobalamins (3d6 electronic configuration)
can be reduced to Co(II) and Co(I).8 Cobalamin in the Co(I) oxi-
dation state (3d8) is four-coordinate and approximately square-
planar; it has two electrons in the d z2 orbital and is a very good
nucleophile.9
The biological function of methylcobalamin (and related
methylcorrinoids) is to act as a coenzyme in enzymatic methyl
Review Articles South African Journal of Science 98, November/December 2002
Fig. 1. Vitamin B12 (cyanocobalamin) and methylcobalamin. For cyanocobalamin
R = –CN and for methylcobalamin R = –CH3.
transfer reactions. Methylcobalamin is the coenzyme for
methionine synthase, which catalyses the transfer of a methyl
group from 5-CH3-tetrahydrofolate (N5-methyltetrahydro-
folate, Fig. 2) to L-homocysteine in order to give L-methionine, as
follows:
cob(I)alamin + 5-CH3-tetrahydrofolate →
CH3-cobalamin + tetrahydrofolate
H 3N +
CH3-cobalamin + CH-CH2-CH2-S– →
–
OOC
H3N+
cob(I)alamin + CH-CH2-CH2-S-CH3
–
OOC
Methionine synthase is found in humans and other mammals
as well as in microorganisms.10
Acetogenic bacteria synthesize acetic acid by reducing carbon
dioxide. In Clostridium thermoaceticum, a corrinoid-dependent
methyltransferase takes part in the formation of acetyl-co-
enzyme A from coenzyme A (Fig. 2). The corrinoid used is
5’-methoxybenzimidazolylcobamide (which has the 5’-methoxy-
benzimidazole base instead of 5,6-dimethylbenzimidazole)
rather than cobalamin. The reactions are as follows:
corrinoid iron sulphur protein + 5-CH3-tetrahydrofolate →
CH3-corrinoid iron sulphur protein + tetrahydrofolate
CH3-corrinoid iron sulphur protein + acetyl-coenzyme A
synthase → corrinoid iron sulphur protein + CH3-acetyl-
coenzyme A synthase
CH3-acetyl-coenzyme A synthase + coenzyme A-SH →
coenzyme A-S-C-CH3
O Mercury(II) also complexes with the nitrogen atom of the
The corrinoid that reacts with 5-CH3-tetrahydrofolate is in the
Co(I) oxidation state.11
Corrinoid proteins are involved in the synthesis of methane
from carbon dioxide and hydrogen and from acetate by
methanogenic archaea. One of the steps in this pathway in
Methanobacterium thermoautotrophicum is the formation of
methyl-coenzyme M from 5-CH3-tetrahydromethanopterin
569
(N5-methyltetrahydromethanopterin) and coenzyme M (Fig. 2),
which is catalysed by a corrinoid-dependent methyltransferase:
5-CH3-tetrahydromethanopterin + H-S-coenzyme M →
tetrahydromethanopterin + CH3-S-coenzyme M
The corrinoid used is 5’-hydroxybenzimidazolylcobamide and
it is active in the Co(I) oxidation state.12
In the reaction sequences of both methionine synthase10 and
the corrinoid-dependent methyltransferase of Clostridium
thermoaceticum,11 the Co(I) acts as a nucleophile towards the
methyl group of 5-CH3-tetrahydrofolate to form a methyl
corrinoid and then the methyl group is transferred to a methyl
acceptor, regenerating Co(I). The methyl corrinoid can be con-
sidered formally as a complex of Co(I) with a methyl carbonium
ion and the Co–C bond is broken by heterolytic cleavage (SN2) in
which the transition state corresponds to (CoI + CH3+).
Methylcobalamin is synthesized and used by many microor-
ganisms and bacteria and is present in the natural environment.
The biological function of methylcobalamin is its action as a
methylating agent and this is obviously useful to the organism.
However, methylcobalamin can also play a role that is harmful to
the environment by methylating mercury(II) to give methyl-
mercury, which is more toxic to higher organisms. Methyl-
cobalamin could methylate mercury(II) in the environment by
two possible routes. First, methylcobalamin of natural origin
could methylate mercury by a purely chemical or abiotic route.
Second, microorganisms or bacteria could be implicated and
methylcobalamin could methylate mercury(II) by means of
enzymatic catalysis using a biotic route. Enzymes using
methylcobalamin or related methylcorrinoids in the process
of biomethylation of natural substrates could react with
mercury(II), resulting in the methylation of mercury.3
Chemical reaction of methylcobalamin with mercury(II)
The reaction of methylcobalamin with mercury(II) in aqueous
solution to give aquocobalamin and methylmercury is as
follows:
CH3-cobalamin + Hg2+ + H2O → H2O-cobalamin + CH3Hg+.
The reaction between methylcobalamin and mercury(II)
occurs under both aerobic and anaerobic conditions.13 The opti-
mum pH for this reaction is 4.5.14 Methylmercury reacts further
with methylcobalamin to give dimethylmercury, (CH3)2Hg, but
this reaction is much slower than the reaction of mercury(II)
with methylcobalamin.15 The methylation of mercury(II) by
methylcobalamin is shown in Fig. 3.
Methylcobalamin can be considered as a complex of Co(III)
with a methyl carbanion and the Co–C bond can be broken by a
reaction in which the transition state corresponds to (CoIII
+CH3–).16 Mercury(II) acts as an electrophile towards the Co–C
F-bond in an SE2 mechanism and heterolytic cleavage of the
Co–C F-bond takes place. The methyl carbanion (CH3–) is trans-
ferred to mercury, giving methylmercury (CH3Hg+).13,14,17–20 The
coordination position on the cobalt occupied by the methyl
group in methylcobalamin is taken up by water, giving aquo-
cobalamin.
5,6-dimethylbenzimidazole base of cobalamin in an equilibrium
reaction. The nitrogen atom is thus removed from coordination
with cobalt, giving the ‘base-off ’ form of methylcobalamin. The
‘base-off ’ form also reacts with mercury(II) to give methyl-
mercury but this reaction is 3000 times slower than the reaction
with the ‘base-on’ form. The coordination of the 5,6-dimethyl-
benzimidazole ligand in the position trans to the methyl group
570 South African Journal of Science 98, November/December 2002 Review Articles

speeds up the transfer of the methyl carbanion

(CH3–) to mercury(II), when compared to the coor-
dination of H2O (or no ligand).13,14,17–20 When the
Co–C bond of methylcobalamin is polarized in
the direction of (CoIII + CH3–) by the ‘pull’ of Hg2+,
the reaction is further promoted by the ‘push’ of the
5,6-dimethylbenzimidazole ligand (which is a
good donor ligand).16,17
In general, transfer of a methyl carbanion to a
metal takes place when the standard reduction po-
tential of the metal (E0) is greater than 0.8 V.18,19 The
E0 for the Hg2+/Hg couple is +0.85 V.1 Both CH3-
tetrahydrofolate and S-adenosylmethionine,
which are (in addition to methylcobalamin) the
most important biological methylating molecules,
transfer the methyl group as a carbonium ion and
so would not be suitable methylators for positive
Hg2+ ions.3,14,21

Methylation of mercury — abiotic or biotic?

There have been many reports of the methylation
of mercury(II) by bacteria under various condi-
tions. 3 , 2 2 , 2 3 In 1968 Wood 6 reported that a
methanogenic bacterium from an aquatic sediment
is capable of using methylcobalamin to methylate
mercury(II) and proposed that transfer of a methyl
group from methylcobalamin to mercury(II) in bio-
logical systems may occur as a non-enzymatic pro-
cess. However, in 1985, Compeau and Bartha24
reported that sulphidogens methylate mercury in
aquatic sediments and that methanogens and
acetogens do not.24 There is controversy about
whether bacteria methylate mercury by an abiotic
or a biotic route. In the abiotic route, the Fig. 2. Tetrahydrofolic acid, tetrahydromethanopterin, coenzyme A and coenzyme M.
methylcobalamin (or methyl corrinoid) is pro-
duced enzymatically but the methylation of mercury(II) occurs from the carbon-3 of serine and that it is transferred to
by a non-enzymatic chemical reaction. The abiotic route is rea- tetrahydrofolate in order to give 5-CH3-tetrahydrofolate. The
sonable because the chemical reaction between methyl- methyl group is transferred from 5-CH3-tetrahydrofolate to a
cobalamin and mercury(II) to give methylmercury takes place cobalt-containing species and the methylated cobalt-containing
fairly rapidly in aqueous solution at slightly acidic to neutral pH.
Also, acetogens and methanogens produce large amounts of
cobalamins as well as other corrinoids25 and these are available
for the methylation of mercury. In the biotic route, bacteria use
their corrinoid-dependent methyltransferase enzymes to
methylate mercury(II); enzymatic catalysis of the methylation of
mercury takes place.
Compeau and Bartha24,26 discovered that sulphate-reducing
bacteria were the most important methylators of mercury in
anoxic aquatic sediments. Strains of Desulphovibrio desulfuricans
(a sulphate-reducing bacterium or sulphidogen) were isolated
and shown to methylate mercury.24,26 Sulphate-reducing bacteria
(such as Desulphovibrio species) use sulphate as an electron
acceptor, reducing it to sulphide; this provides a means of detoxi-
fying mercury(II) by converting it to the insoluble mercuric sul-
phide.4 The identification of D. desulfuricans as bacteria that
methylate mercury was therefore surprising because D. desul-
furicans would be expected to prevent the methylation of mer-
cury.24
Bartha and coworkers 24,26–31 studied the methylation of
mercury by sulphate-reducing bacteria, with the objective of
discovering the methyl donor and finding out if enzymatic catal-
ysis takes place. They proposed, based on radiocarbon incorpo-
ration from pyruvate and serine into methylmercury, that in
D. desulfuricans the methyl group of methylmercury originates Fig. 3. Reaction of methylcobalamin with mercury(II).
Review Articles South African Journal of Science 98, November/December 2002
species then methylates mercury(II).27 The reactions are as
follows:
[Co] Hg(II)
5-CH3-tetrahydrofolate → CH3-Co → CH3-Hg
It was suggested that a cobalamin or a related cobalt porphyrin
was involved in the methylation of mercury(II) by D. desul-
furicans, on the basis of inhibition of mercury methylation
by propyl iodide and reversal of inhibition by light.27 (n-Propyl
iodide reacts with cob(I)alamin to give n-propylcobalamin and
the n-propyl group is removed in the presence of light.8)
In a later paper, Choi and Bartha28 showed that Desulphovibrio
desulfuricans LS contains cobalamin as its only corrinoid. D. desul-
furicans LS was grown in the presence of 57CoCl2 and a corrinoid
was extracted and purified. The corrinoid was determined to be
cyanocobalamin by high-performance liquid chromatography
and 97% of the 57Co radioactivity was associated with cyano-
cobalamin. The identity as cyanocobalamin was confirmed
using UV-visible spectroscopy and fast atom bombardment
mass spectroscopy. Methylcobalamin was prepared from the
cobalamin isolated from D. desulfuricans LS and 14CH3I and was
shown to methylate mercury(II) spontaneously. They con-
cluded that D. desulfuricans LS methylates mercury(II) using
methylcobalamin as the methyl donor. 28 The corrinoid,
5’-methylbenzimidazolylcobamide (which has the 5’-methyl-
benzimidazole base instead of 5,6-dimethylbenzimidazole), is
present in some sulphate-reducing bacteria.32 The methyl form
of 5’-methylbenzimidazolylcobamide (and other corrinoids
containing analogues of 5,6-dimethylbenzimidazole) should
also be capable of methylating mercury.
Choi, Chase and Bartha29 proposed in 1994 that methylation of
mercury(II) by D. desulfuricans LS is enzymatically catalysed.
They isolated a single Co-corrinoid protein with a size of approx-
imately 40 kDa and proposed that this protein is the in vivo
methyl donor in D. desulfuricans LS. They showed that methyla-
tion of mercury(II) by cell extracts of D. desulfuricans LS under
reducing conditions followed Michaelis-Menten kinetics with
a maximum specific activity of 0.73 nmol min–1 (mg of cell
protein)–1. They found that the optimal conditions were pH 6.5
and temperature 35°C and that the activity decreased in the
presence of air. They found that the rate of methylation of
mercury(II) in the presence of cell extracts of D. desulfuricans LS
was much greater than the rate of transmethylation by free
methylcobalamin (600 times greater at pH 7) and that saturation
kinetics were observed; they suggested that these observations
‘proved that in vivo Hg2+ methylation is an enzymatically
catalysed process’.29 However, in order to prove that the
Co-corrinoid protein is the enzymatic catalyst for the methyla-
tion of mercury(II) by methylcobalamin, it is necessary to isolate
the protein and show that it increases the rate of reaction when
compared to the rate of the non-enzymatic reaction.
The transfer of the methyl group from 5-CH3-tetrahydrofolate
can be considered to take place in two steps:29
(i) 5-CH3-tetrahydrofolate + Co-corrinoid-protein → CH3-Co-
corrinoid-protein + tetrahydrofolate
(ii) CH3-Co-corrinoid protein + Hg2+ → Co-corrinoid-protein +
CH3Hg+
Choi, Chase and Bartha29 proposed that step (ii) is enzymati-
cally catalysed. They suggested that either the Co-corrinoid-
protein in step (ii) acts as a methyltransferase enzyme or that a
separate methyltransferase is required. They also suggested that
the methyltransferase could be part of the pathway for the syn-
thesis of acetyl-coenzyme A and take part in the acetyl-coen-
571
zyme A synthase reaction.29 In a later paper, Pak and Bartha31
suggested that the acetyl-coenzyme A synthase reaction, if
reversed, could play a role in the demethylation of mercury by
sulfidogens.31
It appears that other sulphidogens are able to methylate mer-
cury(II). Regnell and coworkers33 proposed that sulphate-
reducing bacteria belonging to the genus Desulphobacter rather
than Desulphovibrio also methylate mercury using methyl-
cobalamin. They based this conclusion on the presence of the
phospholipid fatty acid 10Me16:0 (characteristic of Desulpho-
bacter) in sediment from a freshwater lake contaminated with
mercury and the strong correlation between the amount of
methylmercury, amount of cobalamin and this phospholipid
fatty acid. In Desulphobacter, the fatty acid 10Me16:0 is biosynthe-
sized by the transfer of a methyl group from methionine to the
double bond in a straight-chain monosaturated fatty acid.33 They
suggested that a methyltransferase, using methylcobalamin as a
cofactor and involved in the biosynthesis of 10Me-branched
fatty acids could methylate mercury(II) in this system. An alter-
native suggestion was that acetogenic bacteria, which contain
large amounts of cobalamins, could stimulate the growth of
Desulphobacter, which would then methylate mercury.33
There is strong evidence that sulphidogens do methylate
mercury(II) under certain conditions and that methylcobalamin
is the methyl donor in this process. Whether or not the methyla-
tion of mercury(II) by sulphate-reducing bacteria is due to enzy-
matic catalysis is open to question. I think that, for sulphidogens,
methylcobalamin is probably produced enzymatically but the
methylation of mercury(II) may occur by a non-enzymatic or
abiotic route.
There has been a great deal of controversy about the synthesis
of methylmercury in nature: abiotic versus biotic and methano-
gens versus sulphidogens.34 This controversy has been partially
resolved by a cooperation between two species of bacteria! Pak
and Bartha30 found that cocultures of D. desulfuricans LS (a
sulphidogen) and Methanococcus maripaludis (a methanogen)
grew well on sulphate-free lactate medium and at the same time
they were active in methylating mercury(II). Neither species
could grow individually on the sulphate-free lactate medium
because D. desulfuricans LS could use lactate as its organic sub-
strate but did not have a suitable electron acceptor (no sulphate
present) and M. maripaludis could not use lactate as its organic
substrate. D. desulfuricans LS alone synthesized only a small
amount of methylmercury and M. maripaludis alone did not syn-
thesize methylmercury. D. desulfuricans LS can oxidize lactate to
pyruvate and the pyruvate gives rise to CO2, acetate and hydro-
gen (as reducing equivalents). M. maripaludis, in turn, uses the
acetate as its organic substrate and reduces CO2 using hydrogen.
This is a cooperative relationship because the D. desulfuricans LS
supplies M. maripaludis with acetate, which it needs for growth
and M. maripaludis removes the hydrogen, allowing D. desul-
furicans LS to grow in the absence of the sulphate electron accep-
tor.30 They proposed that growth of sulphidogens and methano-
gens involving an interaction between the two species similar to
that occurring on the sulphate-free lactate medium would
provide suitable conditions for the methylation of mercury(II) in
anoxic freshwater sediments. The sulphidogens that methylate
mercury also produce H2S, which, in turn, inhibits the methyla-
tion of mercury(II). For this reason, situations that permit
sulphidogens to be active without using reduction of sulphates
would be favourable to methylation of mercury(II). Such a situa-
tion is the interspecies transfer of hydrogen and acetate between
sulphidogens and methanogens, which may be important in the
methylation of mercury(II) in the environment.30
572 South African Journal of Science 98, November/December 2002
I thank P.R. Johnson for his careful reading of the manuscript and one of the
reviewers for useful input. The University Research Committee of the University of
the Witwatersrand provided financial support.
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