Enzymes and associated electron transport systems that catalyse the respiratory reduction of nitrogen oxides and oxyanions
603
About: This article is published in Biochimica et Biophysica Acta. The article was published on 12 Dec 1995. and is currently open access.
read more
Chat with Paper
AI Agents for this Paper
Find similar papers on Google Scholar, PubMed and Arxiv
Write a critical review of this paper
Analyze citations of this paper to find unaddressed research gaps
Citations
Cell biology and molecular basis of denitrification.
TL;DR: Denitrification is intimately related to fundamental cellular processes that include primary and secondary transport, protein translocation, cytochrome c biogenesis, anaerobic gene regulation, metalloprotein assembly, and the biosynthesis of the cofactors molybdopterin and heme D1.
The Mononuclear Molybdenum Enzymes
TL;DR: It is now well-established that all molybdenum-containing enzymes other than nitrogenase fall into three large and mutually exclusive families, as exemplified by the enzymes xanthine oxidation, sulfite oxidase, and DMSO reductase; these enzymes represent the focus of the present account.
Copper Active Sites in Biology
Edward I. Solomon,David E. Heppner,Esther M. Johnston,Jake W. Ginsbach,Jordi Cirera,Munzarin F. Qayyum,Matthew T. Kieber-Emmons,Christian H. Kjaergaard,Ryan G. Hadt,Li Tian +9 more
TL;DR: This review presents in depth discussions of all these classes of Cu enzymes and the correlations within and among these classes, as well as the present understanding of the enzymology, kinetics, geometric structures, electronic structures and the reaction mechanisms these have elucidated.
Metalloproteins containing cytochrome, iron-sulfur, or copper redox centers.
Jing Liu,Saumen Chakraborty,Parisa Hosseinzadeh,Yang Yu,Shiliang Tian,Igor D. Petrik,Ambika Bhagi,Yi Lu +7 more
TL;DR: Through this review, structural features responsible for their redox properties are examined, including knowledge gained from recent progress in fine-tuning the redox centers.
796
NITRATE REDUCTASE STRUCTURE, FUNCTION AND REGULATION: Bridging the Gap between Biochemistry and Physiology.
Wilbur H. Campbell
- 01 Jun 1999
TL;DR: A complete three-dimensional dimeric NR structure model was built from structures of sulfite oxidase and cytochrome b reductase, and key active site residues have been investigated.
791
References
Protein-mediated electron transfer
TL;DR: The concept of proteins as conducting glassees is reviewed in this article, in the light of recent experimental evidence on biological electron-transfer rates and their dependence on driving force, reorganization energy, and the distance and coupling between partners.
38
Positional isotopic equivalence of nitrogen in N2O produced by the denitrifying bacterium Pseudomonas stutzeri. Indirect evidence for a nitroxyl pathway.
E A Garber,T C Hollocher +1 more
TL;DR: It was determined that themass spectrometric abundance of 14N15NO was about equal to that of 15N14NO in 14,15N2O by examination of the abundances of 14NO+, 15NO+, and 15N2+ that arose from the fragmentation of N2O+ species in the mass spectrometer.
37
Molecular characterization of nosA, a Pseudomonas stutzeri gene encoding an outer membrane protein required to make copper-containing N2O reductase.
TL;DR: A Pseudomonas stutzeri gene (nosA) encoding an outer membrane protein was cloned into the broad-host-range vector pRK290 and expressed in a mutant lacking the protein, suggesting a homologous function: interaction with a periplasmic protein or uptake of a specific substrate.
37
Selection, expression, and nucleotide sequencing of the glutamate dehydrogenase gene of Peptostreptococcus asaccharolyticus.
B Snedecor,H Chu,E Chen +2 more
TL;DR: The sequence similarity of this protein to the mammalian glutamate dehydrogenases, which accept both NADP and NAD, is greater than its similarity to the bacterial NADP-specific dehydrogenase, suggesting that this NAD-specific bacterial glutamate dehydration enzyme diverged separately from the line leading to the dual-specificity mammalian glutamate dehydrationases.
37
Detection of a nitrous oxide reductase structural gene in Rhizobium meliloti strains and its location on the nod megaplasmid of JJ1c10 and SU47.
Yiu-Kwok Chan,Roger Wheatcroft +1 more
TL;DR: Zumft et al. as discussed by the authors detected the denitrification enzyme, nitrous oxide reductase (EC 1.7.6), in rhizobium meliloti and other gram-negative bacteria by hybridization to an internal 1.2-kb PstI fragment of the structural gene (nosZ) cloned from Pseudomonas stutzeri Zobell (W.G. Zumft, A. Viebrock-Sambale, and C. Braun, Eur. Biochem. 192:591-599, 1990).
37