Hydrogenase (NAD+, ferredoxin)

In today's world, Hydrogenase (NAD+, ferredoxin) has gained transcendental relevance in all areas. From the personal to the professional level, Hydrogenase (NAD+, ferredoxin) has been the subject of interest and debate in today's society. Its impact has transcended borders and has generated all kinds of reflections and analyzes by experts and ordinary citizens. In this article, we will further explore the meaning and importance of Hydrogenase (NAD+, ferredoxin), as well as its influence on our daily lives. Since its appearance, Hydrogenase (NAD+, ferredoxin) has been the subject of numerous studies and discussions seeking to understand its true nature and its impact on society. Throughout this text, we will explore different perspectives and points of view on Hydrogenase (NAD+, ferredoxin), with the aim of shedding light on a topic that concerns us all.

Hydrogenase (NAD+, ferredoxin)
Identifiers
EC no.1.12.1.4
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins

Hydrogenase (NAD+, ferredoxin) (EC 1.12.1.4, bifurcating hydrogenase) is an enzyme with systematic name hydrogen:NAD+, ferredoxin oxidoreductase.[1][2] This enzyme catalyses the following chemical reaction

2 H2 + NAD+ + 2 oxidized ferredoxin 5 H+ + NADH + 2 reduced ferredoxin

The enzyme from Thermotoga maritima contains a cluster (H-cluster) and iron-sulfur clusters. I

References

  1. ^ Verhagen MF, O'Rourke T, Adams MW (August 1999). "The hyperthermophilic bacterium, Thermotoga maritima, contains an unusually complex iron-hydrogenase: amino acid sequence analyses versus biochemical characterization". Biochimica et Biophysica Acta. 1412 (3): 212–29. doi:10.1016/s0005-2728(99)00062-6. PMID 10482784.
  2. ^ Schut GJ, Adams MW (July 2009). "The iron-hydrogenase of Thermotoga maritima utilizes ferredoxin and NADH synergistically: a new perspective on anaerobic hydrogen production". Journal of Bacteriology. 191 (13): 4451–7. doi:10.1128/JB.01582-08. PMC 2698477. PMID 19411328.