3ozw: Difference between revisions
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{{STRUCTURE_3ozw| PDB=3ozw | SCENE= }} | {{STRUCTURE_3ozw| PDB=3ozw | SCENE= }} | ||
===The Crystal Structure of flavohemoglobin from R. eutrophus in complex with ketoconazole=== | ===The Crystal Structure of flavohemoglobin from R. eutrophus in complex with ketoconazole=== | ||
{{ABSTRACT_PUBMED_21210640}} | |||
==Function== | |||
[[http://www.uniprot.org/uniprot/HMP_RALEH HMP_RALEH]] Is involved in NO detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) and NAD(P)H to convert NO to nitrate, which protects the bacterium from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress.[HAMAP-Rule:MF_01252] In the presence of oxygen and NADH, FHP has NADH oxidase activity, which leads to the generation of superoxide and H(2)O(2), both in vitro and in vivo, and it has been suggested that FHP might act as an amplifier of superoxide stress. Under anaerobic conditions, FHP also exhibits nitric oxide reductase and FAD reductase activities. However, all these reactions are much lower than NOD activity.[HAMAP-Rule:MF_01252] | |||
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==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
<ref group="xtra">PMID: | <ref group="xtra">PMID:021210640</ref><references group="xtra"/><references/> | ||
[[Category: Cupriavidus necator]] | [[Category: Cupriavidus necator]] | ||
[[Category: Nitric oxide dioxygenase]] | [[Category: Nitric oxide dioxygenase]] | ||
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[[Category: Hammi, E El.]] | [[Category: Hammi, E El.]] | ||
[[Category: Warkentin, E.]] | [[Category: Warkentin, E.]] | ||
[[Category: Alpha/beta fold]] | |||
[[Category: Antiparallel beta-barrel]] | |||
[[Category: Fad-]] | |||
[[Category: Globin fold]] | |||
[[Category: Hem-]] | |||
[[Category: Lipid binding protein]] | |||
[[Category: Nad- binding domain]] | |||