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Literature summary for 1.12.1.4 extracted from

  • Birrell, J.A.; Laurich, C.; Reijerse, E.J.; Ogata, H.; Lubitz, W.
    Importance of hydrogen bonding in fine tuning the [2Fe-2S] cluster redox potential of HydC from Thermotoga maritima (2016), Biochemistry, 55, 4344-4355 .
    View publication on PubMed
Search for more literature for 1.12.1.4

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Thermotoga maritima

Protein Variants

Protein Variants Comment Organism
A85P the mutant has an altered reduction potential compared to the wild type enzyme Thermotoga maritima
V131N the mutant has an altered reduction potential compared to the wild type enzyme Thermotoga maritima

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
H2 + NAD+ + oxidized ferredoxin Thermotoga maritima
-
 H+ + NADH + reduced ferredoxin
-
 ?
H2 + NAD+ + oxidized ferredoxin Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
 H+ + NADH + reduced ferredoxin
-
 ?

Organism

Organism UniProt Comment Textmining
Thermotoga maritima
-
-
-
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
-
-

Purification (Commentary)

Purification (Comment) Organism
streptactin column chromatography Thermotoga maritima

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
H2 + NAD+ + oxidized ferredoxin
-
 Thermotoga maritima H+ + NADH + reduced ferredoxin
-
 ?
H2 + NAD+ + oxidized ferredoxin
-
 Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589 H+ + NADH + reduced ferredoxin
-
 ?

Synonyms

Synonyms Comment Organism
HydC gamma subunit Thermotoga maritima
NAD(P)+-linked [FeFe]-hydrogenase
-
 Thermotoga maritima

Cofactor

Cofactor Comment Organism Structure
[2Fe-2S]-center
-
 Thermotoga maritima