Reaction participants Show >> << Hide
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Name help_outline
a menaquinol
Identifier
CHEBI:18151
Charge
0
Formula
C11H10O2(C5H8)n
Search links
Involved in 53 reaction(s)
Find proteins in UniProtKB for this molecule
Form(s) in this reaction:
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Identifier: RHEA-COMP:9539Polymer name: a menaquinolPolymerization index help_outline nFormula C11H10O2(C5H8)nCharge (0)(0)nMol File for the polymer
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- Name help_outline nitrate Identifier CHEBI:17632 (Beilstein: 3587575; CAS: 14797-55-8) help_outline Charge -1 Formula NO3 InChIKeyhelp_outline NHNBFGGVMKEFGY-UHFFFAOYSA-N SMILEShelp_outline [O-][N+]([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 26 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Name help_outline
a menaquinone
Identifier
CHEBI:16374
(CAS: 11032-49-8)
help_outline
Charge
0
Formula
(C5H8)nC11H8O2
Search links
Involved in 47 reaction(s)
Find proteins in UniProtKB for this molecule
Form(s) in this reaction:
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Identifier: RHEA-COMP:9537Polymer name: a menaquinonePolymerization index help_outline nFormula C11H8O2(C5H8)nCharge (0)(0)nMol File for the polymer
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- Name help_outline H2O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,204 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline nitrite Identifier CHEBI:16301 (CAS: 14797-65-0) help_outline Charge -1 Formula NO2 InChIKeyhelp_outline IOVCWXUNBOPUCH-UHFFFAOYSA-M SMILEShelp_outline [O-]N=O 2D coordinates Mol file for the small molecule Search links Involved in 79 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:29127 | RHEA:29128 | RHEA:29129 | RHEA:29130 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
UniProtKB help_outline |
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MetaCyc help_outline | ||||
EcoCyc help_outline |
Related reactions help_outline
Specific form(s) of this reaction
More general form(s) of this reaction
Publications
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NapGH components of the periplasmic nitrate reductase of Escherichia coli K-12: location, topology and physiological roles in quinol oxidation and redox balancing.
Brondijk T.H., Nilavongse A., Filenko N., Richardson D.J., Cole J.A.
Nap (periplasmic nitrate reductase) operons of many bacteria include four common, essential components, napD, napA, napB and napC (or a homologue of napC ). In Escherichia coli there are three additional genes, napF, napG and napH, none of which are essential for Nap activity. We now show that del ... >> More
Nap (periplasmic nitrate reductase) operons of many bacteria include four common, essential components, napD, napA, napB and napC (or a homologue of napC ). In Escherichia coli there are three additional genes, napF, napG and napH, none of which are essential for Nap activity. We now show that deletion of either napG or napH almost abolished Nap-dependent nitrate reduction by strains defective in naphthoquinone synthesis. The residual rate of nitrate reduction (approx. 1% of that of napG+ H+ strains) is sufficient to replace fumarate reduction in a redox-balancing role during growth by glucose fermentation. Western blotting combined with beta-galactosidase and alkaline phosphatase fusion experiments established that NapH is an integral membrane protein with four transmembrane helices. Both the N- and C-termini as well as the two non-haem iron-sulphur centres are located in the cytoplasm. An N-terminal twin arginine motif was shown to be essential for NapG function, consistent with the expectation that NapG is secreted into the periplasm by the twin arginine translocation pathway. A bacterial two-hybrid system was used to show that NapH interacts, presumably on the cytoplasmic side of, or within, the membrane, with NapC. As expected for a periplasmic protein, no NapG interactions with NapC or NapH were detected in the cytoplasm. An in vitro quinol dehydrogenase assay was developed to show that both NapG and NapH are essential for rapid electron transfer from menadiol to the terminal NapAB complex. These new in vivo and in vitro results establish that NapG and NapH form a quinol dehydrogenase that couples electron transfer from the high midpoint redox potential ubiquinone-ubiquinol couple via NapC and NapB to NapA. << Less
Biochem. J. 379:47-55(2004) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.