Environmental Engineering Reference
In-Depth Information
The
Drm. acetoxidans
triheme cytochrome
c
7
is rapidly reduced by the
D. vulgaris
H [Fe] hydrogenase and it can completely reduce polysulfide with a
very high specific activity of 20
moles of hydrogen consumed/min/mg protein
[
151
]. This activity is twice as high as that reported for the purified tetraheme
cytochrome
c
3
with the highest specific SR activity from
Dsm. norvegicum
[
26
,
147
]. These results indicate that cytochrome
c
7
is probably the true terminal sulfur
reductase in
Drm. acetoxidans
but the physiological electron donor for this triheme
protein remains to be found.
μ
3.1.4 Sulfur Oxidoreductase from Sulfurospirillum deleyianum
The
S. deleyianum
DSM 6946 sulfur oxidoreductase (SR) is a constitutive cyto-
plasmic enzyme. The
S. deleyianum
SR is energized by a [Ni-Fe] hydrogenase and
is several times more active in crude extracts than in other sulfur-reducing
eubacteria [
27
]. Sulfur reduction is enhanced by the presence of thiols and the SR
contains at least one [4Fe-4S] center but no
b
-or
c
-type cytochromes [
27
].
3.2 Archaebacterial Sulfur Reductase
3.2.1 Membraneous Sulfur Reductase Complex from Acidianus
ambivalens
The acidophilic
Acidianus
(
A.
)
ambivalens
DSM 3772 grows on elemental sulfur at
80
C. A hydrogenase-sulfur reductase complex (SR) has been isolated from the
membrane of
A. ambivalens
and the Sr subunits are similar to those found in
W. succinogenes
[
25
] (Figure
5
). SR is a molybdoenzyme belonging to the DMSO
reductase family [
152
]. The SR gene cluster consists of 5 subunits. The s
reA
gene
produces a 110 kDa protein that has binding motifs for a [4Fe-4S] center. The
sreB
gene encodes for a protein rich in cysteines and could coordinate a [4Fe-4S] center.
SreC is a hydrophobic protein that stabilizes the SR into the membrane and the role
for SreD is unresolved at this time. The hydrogenase gene cluster consists of 12 genes
and 3 of these encode for structural proteins. The HynL subunit contains nickel and
the subunit HynS contains several [Fe-S] binding motifs, making this a [Ni-Fe]
hydrogenase. The third structural gene, Isp1, is an integral membrane protein and
serves to bind the 2 other subunits into the membrane. The quinone, presumed to be
sulfolobusquinone, transfers electrons from hydrogenase to the SR.
3.2.2 Sulfur-Reducing Complex from Pyrodictium abyssi
Extensive studies on sulfur reduction have been performed with
Pyrococcus
(
P.
)
furiosus
,
A. ambivalens
,
Py. abyssi
, and
Py. brockii
as model organisms. The
mechanism of sulfur reduction with H
2
, in some members of the
Crenarchaeota
Search WWH ::
Custom Search