Results 191 to 200 of about 503,441 (367)

Prokaryotic Nitrate Reduction: Molecular Properties and Functional Distinction among Bacterial Nitrate Reductases

open access: yesJournal of Bacteriology, 1999
C. Moreno-Vivián   +4 more
semanticscholar   +1 more source

Proteomics of Nitrotyrosine: Integrating Mass Spectrometry and Immunodetection in Redox‐Driven Pathology

open access: yesMass Spectrometry Reviews, EarlyView.
ABSTRACT Nitrooxidative stress, driven by excess reactive nitrogen species like peroxynitrite, contributes to the pathogenesis of many chronic diseases. Among its molecular footprints, 3‐nitrotyrosine (3NT) has emerged as a biologically relevant marker of protein nitration.
Brîndușa Alina Petre
wiley   +1 more source

Rieske Iron–Sulfur Cluster Proteins From an Anaerobic Ammonium Oxidizer Suggest Unusual Energetics in Their Parent Rieske/Cytochrome b Complexes

open access: yesProteins: Structure, Function, and Bioinformatics, EarlyView.
ABSTRACT Anaerobic ammonium‐oxidizing (anammox) bacteria employ a unique, hydrazine‐based pathway to obtain energy from nitrite and ammonium. These organisms possess distinct Rieske/cytochrome b complexes whose precise role in anammox metabolism remains unclear, but which have been proposed to include the generation of NAD(P)H.
David Hauser   +4 more
wiley   +1 more source

Nitrate Reductase. V

open access: yesNippon kagaku zassi, 1950
Fujio Egami   +3 more
openaire   +2 more sources

Look on the positive side! The orientation, identification and bioenergetics of 'Archaeal' membrane-bound nitrate reductases.

open access: yesFEMS Microbiology Letters, 2007
R. M. Martínez-Espinosa   +6 more
semanticscholar   +1 more source

Development of selective growth media for denitrifying bacteria using an evolutionary algorithm: a strategy outline [PDF]

open access: yes, 2005
Boon, Nico   +5 more
core  

Structure and Mechanism of PhdC, a Prenylated‐Flavin Maturase

open access: yesProteins: Structure, Function, and Bioinformatics, EarlyView.
ABSTRACT Prenylated flavin mononucleotide (prFMN) is a modified flavin cofactor required by the UbiD family of (de)carboxylase enzymes. While the reduced prFMNH2 form is produced by the flavin prenyltransferase UbiX, the corresponding two‐electron oxidized prFMNiminium form is required to support UbiD catalysis. Thus, oxidative maturation of prFMNH2 is
Dominic R. Whittall   +4 more
wiley   +1 more source

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