CcNiR: Difference between revisions

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NO2- + 4 H+ + 6 ferricytochrome c = NH4+ + 6 ferrocytochrome c + 2 H2O

The physiological form of the enzyme is believed to be a double trimer of 2 NrfA and 1 NrfH subunits. The catalytic subunit NrfA is a periplasmic membrane-associated pentaheme cytochrome c where the short distances between <scene name='CcNiR/Hemes3/2'>hemes</scene> allow a fast and efficient electron transfer. The active site has been reported as an unusual lysine-coordinated high-spin heme. NrfH is a small membrane-bound cytochrome comprising four c-type heme groups and it serves a double purpose. On one hand, it anchors the catalytic subunits to the membrane. On the other hand, it serves as a quinol oxidase, transferring electrons from the quinone pool to the catalytic subunits. <ref>pmid 14511372</ref> <ref>pmid 12618432</ref> <ref>pmid 8798514</ref> <ref>pmid 17207484</ref> <ref>pmid 20689707</ref> <ref>pmid 17207484</ref>

The physiological form of the enzyme is believed to be a double trimer of 2 NrfA and 1 NrfH subunits. The catalytic subunit NrfA is a periplasmic membrane-associated pentaheme cytochrome c where the short distances between <scene name='CcNiR/Hemes3/3'>hemes</scene> allow a fast and efficient electron transfer. The active site has been reported as an unusual lysine-coordinated high-spin heme. NrfH is a small membrane-bound cytochrome comprising four c-type heme groups and it serves a double purpose. On one hand, it anchors the catalytic subunits to the membrane. On the other hand, it serves as a quinol oxidase, transferring electrons from the quinone pool to the catalytic subunits. <ref>pmid 14511372</ref> <ref>pmid 12618432</ref> <ref>pmid 8798514</ref> <ref>pmid 17207484</ref> <ref>pmid 20689707</ref> <ref>pmid 17207484</ref>

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Revision as of 12:05, 6 September 2012 view source Gabriela Almeida (talk \| contribs) 52 edits No edit summary ← Older edit		Revision as of 12:10, 6 September 2012 view source Gabriela Almeida (talk \| contribs) 52 edits No edit summary Newer edit →
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	NO2- + 4 H+ + 6 ferricytochrome c = NH4+ + 6 ferrocytochrome c + 2 H2O		NO2- + 4 H+ + 6 ferricytochrome c = NH4+ + 6 ferrocytochrome c + 2 H2O

	The physiological form of the enzyme is believed to be a double trimer of 2 NrfA and 1 NrfH subunits. The catalytic subunit NrfA is a periplasmic membrane-associated pentaheme cytochrome c where the short distances between <scene name='CcNiR/Hemes3/2'>hemes</scene> allow a fast and efficient electron transfer. The active site has been reported as an unusual lysine-coordinated high-spin heme. NrfH is a small membrane-bound cytochrome comprising four c-type heme groups and it serves a double purpose. On one hand, it anchors the catalytic subunits to the membrane. On the other hand, it serves as a quinol oxidase, transferring electrons from the quinone pool to the catalytic subunits. <ref>pmid 14511372</ref> <ref>pmid 12618432</ref> <ref>pmid 8798514</ref> <ref>pmid 17207484</ref> <ref>pmid 20689707</ref> <ref>pmid 17207484</ref>		The physiological form of the enzyme is believed to be a double trimer of 2 NrfA and 1 NrfH subunits. The catalytic subunit NrfA is a periplasmic membrane-associated pentaheme cytochrome c where the short distances between <scene name='CcNiR/Hemes3/3'>hemes</scene> allow a fast and efficient electron transfer. The active site has been reported as an unusual lysine-coordinated high-spin heme. NrfH is a small membrane-bound cytochrome comprising four c-type heme groups and it serves a double purpose. On one hand, it anchors the catalytic subunits to the membrane. On the other hand, it serves as a quinol oxidase, transferring electrons from the quinone pool to the catalytic subunits. <ref>pmid 14511372</ref> <ref>pmid 12618432</ref> <ref>pmid 8798514</ref> <ref>pmid 17207484</ref> <ref>pmid 20689707</ref> <ref>pmid 17207484</ref>