Environmental Engineering Reference
In-Depth Information
Ar. veneficus
grows with dissimilatory sulfite or thiosulfate reduction but is
unable to couple growth to the transfer of electrons from the electron donor to
sulfate [
123
]. The Dsr gene locus of
Ar. profundus
has
dsrA
contiguous to
dsrB
[
112
]. The DsrD, as product of
Ar. profundus dsrD,
is projected to be about 9.3 kDa
and would be comparable to the
subunit present in the dSiR of
Desulfovibrio
species where it functions in sulfite-binding [
108
]. Downstream of
dsrABD
in both
Archaeoglobus
species is a gene for ferredoxin and this is significant because
ferredoxin may be the electron donor for enzymatic sulfite reduction.
ʳ
2.4.2 Oxy-Sulfur Reductases in Non-sulfate Reducers
There are several genera of bacteria that are capable of reducing tetrathionate,
thiosulfate, and sulfite to H
2
S (see reactions
11
,
12
, and
13
), respectively. Sulfite, an
intermediate of dissimilatory sulfate reduction, is readily utilized by SRB and the
metabolism of tetrathionate or thiosulfate with the production of sulfide is covered
in Section
2.1
. In the environment, thiosulfate is found in marine and freshwater
sediments [
124
] and in the lumen of mammalian large intestine [
125
]. Tetrathionate
is present in soils, where SRB are growing [
126
], and is produced in the gut as a
result of inflammatory response [
127
]. Several microorganisms that are taxonom-
ically unrelated have enzymes that function under anaerobic conditions as facili-
tating sulfite respiration (reactions
11
,
12
, and
13
)[
20
].
S
4
O
2
6
2e
2S
2
O
2
3
E
0'
þ
!
¼
þ
170 mV 41
½
ð
11
Þ
S
2
O
2
2H
þ
þ
2e
!
SO
2
3
E
0'
þ
þ
H
2
S
¼
402 mV 41
½
ð
12
Þ
3
SO
2
3
8H
þ
þ
6e
!
3H
2
O
0'
þ
H
2
S
þ
¼
160 mV 41
½
ð
13
Þ
The sulfite reductase, Fsr, present in
Methanocaldococcus jannaschii
(M
r
70 kDa) could have arisen from gene fusion since the N-terminal part of the enzyme
is a homolog of the
ʲ
subunit of coenzyme F
420
-reducing hydrogenase (FpoF or
FqoF) while the C-terminal half has homology to DsrA and DsrB of the siroheme-
containing dSiR [
128
]. A homolog of this bifunctional sulfite reductase from
Methanocaldococcus jannaschii
is also present in
Methanopyrus kandleri
and
Methanococcoides burtonii
[
129
].
The dissimilatory sulfite reductase, dSiR, of
Bilophila wadsworthia
has a
ʱ
2
ʲ
2
ʳ
n
(n
2) multimeric structure. This enzyme has an absorption maximum at 630 nm
[
130
] indicating that it is a desulfoviridin-type enzyme. The
ʱ
subunit (M
r
49 kDa)
contains the siroheme-[4Fe-4S] while the
ʲ
subunit is a fusion protein resulting from fused
dsrB
and
dsrD
genes. Based on
phylogenic analysis,
Bilophila wadsworthia
is closely related to
D. desulfuricans
Essex 6 and at one time may have been a dissimilatory sulfate reducer [
130
].
An inducible dissimilatory sulfite reductase in
Clostridium pasteurianum
couples
growth to the reduction of sulfite [
131
].Theisolatedenzyme(M
r
83.6 kDa), has an
ʲ
subunit polypeptide is 54 kDa. The
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