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5,10-Methenyltetrahydromethanopterin hydrogenase
CLASS OF ENZYMES
5,10-methenyltetrahydromethanopterin hydrogenase; EC 1.12.98.2; Hydrogen:5,10-methenyltetrahydromethanopterin oxidoreductase; Iron-sulfur cluster free hydrogenase
The 5,10-methenyltetrahydromethanopterin hydrogenase (or Hmd), the so-called iron-sulfur cluster-free hydrogenase, is an enzyme found in methanogenic archea such as Methanothermobacter marburgensis. It was discovered and first characterized by the Thauer group at the Max Planck Institute in Marburg.
NiFe hydrogenase
![Figure 6. Illustration of the [NiFe] hydrogenase active site inhibited by CO. Top-down view (left). Side view (center). Chemdraw depiction of the inhibited active site (right). The figure was prepared with Jmol<ref name="Jmol"/> and coordinates from 1UBK.pdb. Ni ion = green; Fe ion = orange; sulfur = yellow; oxygen = red; carbon = dark gray; nitrogen = blue.](https://commons.wikimedia.org/wiki/Special:FilePath/NiFe-CO inhibited.jpg?width=200 "Figure 6. Illustration of the [NiFe] hydrogenase active site inhibited by CO. Top-down view (left). Side view (center). Chemdraw depiction of the inhibited active site (right). The figure was prepared with Jmol<ref name=\"Jmol\"/> and coordinates from 1UBK.pdb. Ni ion = green; Fe ion = orange; sulfur = yellow; oxygen = red; carbon = dark gray; nitrogen = blue.")
![The active site of [NiFe] hydrogenase in the oxidized form. L refers to non-protein ligand (1 C≡O and 2 <sup>−</sup>C≡N). X can be an [[oxide]], [[sulfur]], [[hydroperoxide]], or a [[hydroxide]].](https://commons.wikimedia.org/wiki/Special:FilePath/Nickel Iron Hydrogenase Active Site.png?width=200 "The active site of [NiFe] hydrogenase in the oxidized form. L refers to non-protein ligand (1 C≡O and 2 <sup>−</sup>C≡N). X can be an [[oxide]], [[sulfur]], [[hydroperoxide]], or a [[hydroxide]].")
![Figure 5. Different redox states of [NiFe] hydrogenase's metal active site. The redox states in the <span style="color:red">red</span> are the '''inactive redox states'''. The redox states in the <span style="color:green">green</span> are the '''active redox states'''. (Adapted from <ref name="OgataDaltonTrans" />).](https://commons.wikimedia.org/wiki/Special:FilePath/Redox states of NiFe hydrogenase.png?width=200 "Figure 5. Different redox states of [NiFe] hydrogenase's metal active site. The redox states in the <span style=\"color:red\">red</span> are the '''inactive redox states'''. The redox states in the <span style=\"color:green\">green</span> are the '''active redox states'''. (Adapted from <ref name=\"OgataDaltonTrans\" />).")
A MICROBIAL ENZYME COMPLEX WHICH CONTAINS NICKEL AND IRON IN ITS ACTIVE SITE. IN ACETOMICROBIUM FLAVIDUM IT IS AN ALPHA 2 BETA 2 TETRAMER.
User:CHEM8240edpt/sandbox/sandbox; Wikipedia talk:Articles for creation/NiFe Hydrogenase; NiFe Hydrogenase; Nickel-iron hydrogenase
[NiFe] hydrogenase is a type of hydrogenase, which is an oxidative enzyme that reversibly converts molecular hydrogen in prokaryotes including Bacteria and Archaea. The catalytic site on the enzyme provides simple hydrogen-metabolizing microorganisms a redox mechanism by which to store and utilize energy via the reaction shown in Figure 1.
Ferredoxin hydrogenase
CLASS OF ENZYMES
EC 1.12.7.2; EC 1.18.99.1; Hydrogen:ferredoxin oxidoreductase
In enzymology, ferredoxin hydrogenase (), also referred to as [Fe-Fe] hydrogenase, H2 oxidizing hydrogenase, H2 producing hydrogenase, bidirectional hydrogenase, hydrogenase (ferredoxin), hydrogenlyase, and uptake hydrogenase, is found in Clostridium pasteurianum, Clostridium acetobutylicum, Chlamydomonas reinhardtii, and other organisms. The systematic name of this enzyme is hydrogen:ferredoxin oxidoreductase
