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Information on EC 1.2.2.1 - formate dehydrogenase (cytochrome) for references in articles please use BRENDA:EC1.2.2.1Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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The enzyme appears in viruses and cellular organisms
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formate dehydrogenase (cytochrome)
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formate + 2 ferricytochrome b1 = CO2 + 2 ferrocytochrome b1 + 2 H+
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Glyoxylate and dicarboxylate metabolism
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formate:ferricytochrome-b1 oxidoreductase
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dehydrogenase, formate (cytochrome)
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formate dehydrogenase
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formate dehydrogenase-N
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isozyme
formate dehydrogenase-O
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isozyme
formate:cytochrome b1 oxidoreductase
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formate:phenazine methosulfate oxidoreductase
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respiratory formate dehydrogenase
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respiratory formate dehydrogenases are redox enzymes that comprise three subunits: a molybdenum cofactor- and FeS cluster-containing catalytic subunit, an electron-transferring ferredoxin, and a membrane-integral cytochrome b
FDH
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brenda
N.C.T.C. 6750
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brenda
N.C.T.C. 6750
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brenda
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formate + ferricytochrome b
CO2 + ferrocytochrome b
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additional information
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crude extract of Escherichia coli is investigated for formic dehydrogenase activity. The extract is very active with methylene blue in the presence of formate. Spectroscopic examination shows that the formic dehydrogenase of the extract reacts normally with O2 through cytochrome b
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cytochrome c
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in its purest state the enzyme contains one molecule of cytochrome co-ordinated by two histidine side chains in the oxidized state
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Se
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enzyme from cells grown in selenite contains selenium, covalently bound to the largest subunit
Iron
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enzyme contains an iron-sulfur centre
Iron
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2 mol haeme per mol enzyme, non-haeme iron has not been routinely determined, enzyme contains [3Fe-4S] cluster
Molybdenum
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enzyme contains molybdenum
Molybdenum
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1.4 mol per mol enzyme
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additional information
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FdhE binds to the molybdoprotein subunits (FdnG and FdoG) of the respiratory formate dehydrogenase
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preparation I, 30°C
752
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preparation II, 30°C
760
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preparation III, 30°C
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cytoplasmic membrane. Transmembranous locations of the 32000 Da subunit and the 110000 Da subunit
brenda
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brenda
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addition of sodium dithionite stabilizes the enzyme
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663912
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A0A0E1CIM6_KLEPN
294
32224
TrEMBL
A0A2D7RMF6_9GAMM
261
29052
TrEMBL
A0A2E6VGQ7_9GAMM
394
43502
TrEMBL
A0A090NHC7_SHIDY
211
24606
TrEMBL
A0A0A6ZSK4_SHIDY
282
31888
TrEMBL
B9NT67_9RHOB
169
18174
TrEMBL
A0A0A6ZSK8_SHIDY
223
26139
TrEMBL
C7C9E7_METED
Methylobacterium extorquens (strain DSM 6343 / CIP 106787 / DM4)
980
107730
TrEMBL
W8V2L3_KLEPN
211
24703
TrEMBL
Q2LQE4_SYNAS
Syntrophus aciditrophicus (strain SB)
811
90765
TrEMBL
A0A192CE99_ECOLX
195
21368
TrEMBL
A0A192C5Z2_ECOLX
195
21465
TrEMBL
B8CVG3_SHEPW
Shewanella piezotolerans (strain WP3 / JCM 13877)
951
106255
TrEMBL
A0A090NEI1_SHIDY
294
32157
TrEMBL
A0A1E7KTB9_9ACTN
375
40912
TrEMBL
A0A2W2F6J9_9ACTN
387
41809
TrEMBL
Q2LVY7_SYNAS
Syntrophus aciditrophicus (strain SB)
830
92876
TrEMBL
Q2LVY5_SYNAS
Syntrophus aciditrophicus (strain SB)
222
24960
TrEMBL
I5D366_9BURK
276
29720
TrEMBL
E2X354_SHIDY
804
89528
TrEMBL
B6AYR9_9RHOB
134
14285
TrEMBL
A0A2N9AZ84_METEX
345
38048
TrEMBL
A0A0E1CDQ7_KLEPN
803
89932
TrEMBL
A0A2E5Y7C2_9GAMM
386
42435
TrEMBL
Q2LVY6_SYNAS
Syntrophus aciditrophicus (strain SB)
263
29063
TrEMBL
Q2LQE3_SYNAS
Syntrophus aciditrophicus (strain SB)
195
21567
TrEMBL
A0A2E6XK06_9GAMM
197
21697
TrEMBL
A0A2G7TIQ1_RHIML
220
23982
TrEMBL
E2XH05_SHIDY
189
21020
TrEMBL
A0A0E1CEA7_KLEPN
205
22707
TrEMBL
A0A2E1F7E9_9GAMM
398
43782
TrEMBL
A0A090NBT9_SHIDY
195
21511
TrEMBL
A0A090NCK0_SHIDY
195
21456
TrEMBL
A0A090NXE3_SHIDY
809
90017
TrEMBL
W8UZI8_KLEPN
803
89932
TrEMBL
Q2LQE5_SYNAS
Syntrophus aciditrophicus (strain SB)
265
29486
TrEMBL
C5AS21_METEA
Methylobacterium extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1)
198
21673
TrEMBL
A3RRW7_RALSL
998
110717
TrEMBL
A0A0E1CR88_KLEPN
804
89363
TrEMBL
B8CVG7_SHEPW
Shewanella piezotolerans (strain WP3 / JCM 13877)
949
106177
TrEMBL
A0A090NDU5_SHIDY
601
67660
TrEMBL
A0A0A6ZSF1_SHIDY
75
9067
TrEMBL
C7C9E8_METED
Methylobacterium extorquens (strain DSM 6343 / CIP 106787 / DM4)
198
21673
TrEMBL
A0A192C6C9_ECOLX
294
32172
TrEMBL
A0A2E0Z6V8_9CHLR
360
39591
TrEMBL
W8USU7_KLEPN
195
21340
TrEMBL
A0A2E1QDD4_9EURY
157
17097
TrEMBL
A0A2B4N6R2_9BACI
102
10975
TrEMBL
A0A2X1GMG8_BURCE
386
41438
TrEMBL
C5AS22_METEA
Methylobacterium extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1)
345
38096
TrEMBL
A0A192CEV2_ECOLX
211
24606
TrEMBL
A0A0E1CM59_KLEPN
211
24703
TrEMBL
A0A0E1CRS2_KLEPN
195
21340
TrEMBL
A0A0E1CI71_KLEPN
226
26642
TrEMBL
B8CVG2_SHEPW
Shewanella piezotolerans (strain WP3 / JCM 13877)
189
20380
TrEMBL
A0A1D4NBB0_STASA
341
38118
TrEMBL
C7C9E9_METED
Methylobacterium extorquens (strain DSM 6343 / CIP 106787 / DM4)
345
38048
TrEMBL
A0A0N0Z2S7_9ACTN
247
27093
TrEMBL
A0A2E1M9V0_9PROT
270
30063
TrEMBL
W8V7F7_KLEPN
300
33087
TrEMBL
A0A1U1LBR5_9MYCO
75
8256
TrEMBL
E2XH07_SHIDY
195
21511
TrEMBL
B8CVG6_SHEPW
Shewanella piezotolerans (strain WP3 / JCM 13877)
195
20965
TrEMBL
W8UHG9_KLEPN
226
26642
TrEMBL
G5JGT3_9STAP
341
38041
TrEMBL
Q5E543_ALIF1
Aliivibrio fischeri (strain ATCC 700601 / ES114)
340
38485
TrEMBL
Q5E542_ALIF1
202
21866
TrEMBL
Q5E542_ALIF1
Aliivibrio fischeri (strain ATCC 700601 / ES114)
202
21866
TrEMBL
A0A0E1CLQ7_KLEPN
300
33087
TrEMBL
A0A2D5PPJ9_9GAMM
182
20147
TrEMBL
A0A2E5UUH3_9GAMM
390
42998
TrEMBL
Q165C2_ROSDO
Roseobacter denitrificans (strain ATCC 33942 / OCh 114)
960
106217
TrEMBL
A0A090NWN9_SHIDY
189
21020
TrEMBL
C5AS20_METEA
Methylobacterium extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1)
980
107741
TrEMBL
A0A192CFC9_ECOLX
804
89598
TrEMBL
A0A2E8L076_9GAMM
399
43880
TrEMBL
H0FU26_RHIML
75
7874
TrEMBL
A0A2E5KI58_9CHLR
109
11754
TrEMBL
A0A0A6ZSS0_SHIDY
240
27067
TrEMBL
A0A0A7A0L9_SHIDY
195
21456
TrEMBL
W8VIH2_KLEPN
804
89363
TrEMBL
E2X353_SHIDY
300
33132
TrEMBL
Q5E541_ALIF1
Aliivibrio fischeri (strain ATCC 700601 / ES114)
951
106782
TrEMBL
A3RRW8_RALSL
228
23952
TrEMBL
A0A192C6Z0_ECOLX
223
26192
TrEMBL
A0A090NDV2_SHIDY
223
26139
TrEMBL
A0A1D4MR81_STASA
341
38068
TrEMBL
A0A068NMT6_9ACTO
396
43355
TrEMBL
A0A0L8QTP9_9ACTN
369
39511
TrEMBL
Q84FZ7_METEX
198
21673
TrEMBL
A3RRX0_RALSL
384
42375
TrEMBL
A0A090NGN1_SHIDY
300
33132
TrEMBL
W8UUL3_KLEPN
294
32224
TrEMBL
W8VGJ3_KLEPN
205
22707
TrEMBL
Q2LQE6_SYNAS
Syntrophus aciditrophicus (strain SB)
221
24836
TrEMBL
A0A2W4DVL3_9RHIZ
386
42245
TrEMBL
E2X352_SHIDY
211
24606
TrEMBL
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Graham, A.; Boxer, D.H.
The organization of formate dehydrogenase in the cytoplasmic membrane of Escherichia coli
Biochem. J.
195
627-637
1981
Escherichia coli
brenda
Boxer, D.; Malcolm, A.; Graham, A.
Escherichia coli formate to nitrate respiratory pathway: structural analysis
Biochem. Soc. Trans.
10
480-481
1982
Escherichia coli
brenda
Godfrey, C.; Coddington, A.
Purification and properties of formate dehydrogenase from Pseudomonas aeruginosa
Biochem. J.
243
225 - 233
1987
Pseudomonas aeruginosa, Pseudomonas aeruginosa NCTC 6750
brenda
Lueke, I.; Butland, G.; Moore, K.; Buchanan, G.; Lyall, V.; Fairhurst, S.A.; Greenblatt, J.F.; Emili, A.; Palmer, T.; Sargent, F.
Biosynthesis of the respiratory formate dehydrogenases from Escherichia coli: characterization of the FdhE protein
Arch. Microbiol.
190
685-696
2008
Escherichia coli
brenda
Gale, E.F.
Formic dehydrogenase of bacterium coli: its inactivation by oxygen and its protection in the bacterial cell
Biochem. J.
33
1012-1027
1939
Escherichia coli
brenda
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