FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W8545870> ?p ?o ?g. }

• W8545870 endingPage "S46" @default.
• W8545870 startingPage "S45" @default.
• W8545870 abstract "Endogenous metabolism of nitrate to nitrite to nitric oxide (NO) affects numerous biological events in humans, such as blood pressure control and hypoxic vasodilation, yet the molecular mechanism of this transformation remains uncertain and controversial. Nitrate and nitrite conversion to NO are reductive processes, requiring electron and proton transfer reactions, suggesting that oxidoreductase enzymes are involved. Nitrate reduction may occur through a combination of endogenous (i.e. human enzymes) and exogenous (i.e. commensal bacteria) nitrate reductase enzymes, while nitrite reduction to nitric oxide is likely catalyzed by endogenous nitrite reductase enzymes. Several mechanisms have been investigated, yet no conclusive data are available to support a single enzyme as an indispensable component for reduction of nitrite to NO in human tissue. It is likely that different enzyme systems are active in specific tissues under differential hypoxia, pH and co-factor regulatory control. We have identified a novel human nitrite reductase enzyme, which we hypothesize may contribute to mitochondrial reduction of nitrite to NO. The mitochondria amidoxime reducing component (mARC) enzyme is widely expressed in human tissue, but has an undefined physiological function. We hypothesize that mARC catalyzes the NADH-dependent reduction of nitrite to NO. To test this hypothesis the kinetics of nitrite reduction to NO by human mARC was investigated. Recombinant mARC was generated using standard molecular biology techniques, and then isolated using metal affinity chromatography. Site directed mutagenesis was used to change the active site cysteine into alanine. Human cytochrome b5 and cytochrome b5 reductase were also isolated to determine if mARC can utilize NADH as an electron source in conjunction with these enzymes. Nitric oxide chemiluminescence spectroscopy was used to measure NO-formation rates under anaerobic conditions. Our study established that mARC can generate NO from nitrite in the presence of NADH, cytochrome b5, and cytochrome b5 reductase at pH 7.4. The maximum velocity (Vmax) of NO-formation measured was 5 nmoles NO s−1 mg−1 protein. Moreover, mutation of the putative active site cysteine residue to alanine, and substitution of tungsten for molybdenum, completely abolished enzyme activity. The kinetic data supports our hypothesis and establishes that human mARC is capable of catalyzing reduction of nitrite to NO. Moreover, these data suggest that cysteine 270 and molybdenum are important in the transformation of nitrite to NO. Disclosure Supported by institution training grant (T32)." @default.
• W8545870 created "2016-06-24" @default.
• W8545870 creator A5004763246 @default.
• W8545870 creator A5006165632 @default.
• W8545870 creator A5007944034 @default.
• W8545870 creator A5017801434 @default.
• W8545870 creator A5033317704 @default.
• W8545870 creator A5034820453 @default.
• W8545870 creator A5040971909 @default.
• W8545870 creator A5043623665 @default.
• W8545870 creator A5045461759 @default.
• W8545870 creator A5060069444 @default.
• W8545870 creator A5062726882 @default.
• W8545870 creator A5074746000 @default.
• W8545870 creator A5082463683 @default.
• W8545870 creator A5087409511 @default.
• W8545870 date "2013-04-01" @default.
• W8545870 modified "2023-10-16" @default.
• W8545870 title "P74" @default.
• W8545870 doi "https://doi.org/10.1016/j.niox.2013.02.076" @default.
• W8545870 hasPublicationYear "2013" @default.
• W8545870 type Work @default.
• W8545870 sameAs 8545870 @default.
• W8545870 citedByCount "2" @default.
• W8545870 countsByYear W85458702014 @default.
• W8545870 crossrefType "journal-article" @default.
• W8545870 hasAuthorship W8545870A5004763246 @default.
• W8545870 hasAuthorship W8545870A5006165632 @default.
• W8545870 hasAuthorship W8545870A5007944034 @default.
• W8545870 hasAuthorship W8545870A5017801434 @default.
• W8545870 hasAuthorship W8545870A5033317704 @default.
• W8545870 hasAuthorship W8545870A5034820453 @default.
• W8545870 hasAuthorship W8545870A5040971909 @default.
• W8545870 hasAuthorship W8545870A5043623665 @default.
• W8545870 hasAuthorship W8545870A5045461759 @default.
• W8545870 hasAuthorship W8545870A5060069444 @default.
• W8545870 hasAuthorship W8545870A5062726882 @default.
• W8545870 hasAuthorship W8545870A5074746000 @default.
• W8545870 hasAuthorship W8545870A5082463683 @default.
• W8545870 hasAuthorship W8545870A5087409511 @default.
• W8545870 hasConcept C41008148 @default.
• W8545870 hasConceptScore W8545870C41008148 @default.
• W8545870 hasLocation W85458701 @default.
• W8545870 hasOpenAccess W8545870 @default.
• W8545870 hasPrimaryLocation W85458701 @default.
• W8545870 hasRelatedWork W2096946506 @default.
• W8545870 hasRelatedWork W2130043461 @default.
• W8545870 hasRelatedWork W2350741829 @default.
• W8545870 hasRelatedWork W2358668433 @default.
• W8545870 hasRelatedWork W2376932109 @default.
• W8545870 hasRelatedWork W2382290278 @default.
• W8545870 hasRelatedWork W2390279801 @default.
• W8545870 hasRelatedWork W2748952813 @default.
• W8545870 hasRelatedWork W2899084033 @default.
• W8545870 hasRelatedWork W3004735627 @default.
• W8545870 hasVolume "31" @default.
• W8545870 isParatext "false" @default.
• W8545870 isRetracted "false" @default.
• W8545870 magId "8545870" @default.
• W8545870 workType "article" @default.