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Structural Basis of Biological NO Generation by Octaheme Oxidoreductases

Structural Basis of Biological NO Generation by Octaheme Oxidoreductases

http://www.wikidata.org/entity/Q27680746

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The inner workings of the hydrazine synthase multiprotein complex In meso crystal structure of a novel membrane-associated octaheme cytochrome c from the Crenarchaeon Ignicoccus hospitalis Metabolic network analysis reveals microbial community interactions in anammox granules.Nitrosomonas europaea cytochrome P460 is a direct link between nitrification and nitrous oxide emission.Nitric oxide is an obligate bacterial nitrification intermediate produced by hydroxylamine oxidoreductase.Metatranscriptomic evidence of pervasive and diverse chemolithoautotrophy relevant to C, S, N and Fe cycling in a shallow alluvial aquifer.Is there a pathway for N2O production from hydroxylamine oxidoreductase in ammonia-oxidizing bacteria?Unusual respiratory capacity and nitrogen metabolism in a Parcubacterium (OD1) of the Candidate Phyla Radiation.An unexpected reactivity of the P460 cofactor in hydroxylamine oxidoreductase.Immunogold Localization of Key Metabolic Enzymes in the Anammoxosome and on the Tubule-Like Structures of Kuenenia stuttgartiensis.Characterization of Anammox Hydrazine Dehydrogenase, a Key N2-producing Enzyme in the Global Nitrogen Cycle.Epsilonproteobacterial hydroxylamine oxidoreductase (εHao): characterization of a 'missing link' in the multihaem cytochrome c family.Hydroxylamine-dependent anaerobic ammonium oxidation (anammox) by "Candidatus Brocadia sinica".Influences of the heme-lysine crosslink in cytochrome P460 over redox catalysis and nitric oxide sensitivity.Comparative Genomics of Methylomirabilis Species and Description of . Methylomirabilis Lanthanidiphila

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Structural Basis of Biological NO Generation by Octaheme Oxidoreductases

http://www.wikidata.org/entity/Q27680746

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2014年の論文

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2014年論文

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2014年論文

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Structural Basis of Biological NO Generation by Octaheme Oxidoreductases

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Structural Basis of Biological NO Generation by Octaheme Oxidoreductases

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Structural Basis of Biological NO Generation by Octaheme Oxidoreductases

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Structural Basis of Biological NO Generation by Octaheme Oxidoreductases

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Structural Basis of Biological NO Generation by Octaheme Oxidoreductases

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Structural Basis of Biological NO Generation by Octaheme Oxidoreductases

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Structural Basis of Biological NO Generation by Octaheme Oxidoreductases

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Structural Basis of Biological NO Generation by Octaheme Oxidoreductases

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JBC.M113.525147

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Journal of Biological Chemistry

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Structural Basis of Biological NO Generation by Octaheme Oxidoreductases

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Andreas Dietl

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Boran Kartal

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Jan T Keltjens

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Julea N Butt

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Sophie J Marritt

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Thomas R M Barends

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Wouter J Maalcke

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PHENIX: a comprehensive Python-based system for macromolecular structure solution

Multiple sequence alignment with the Clustal series of programs

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

Basic local alignment search tool

Structure of cytochrome c nitrite reductase

Mechanism of the six-electron reduction of nitrite to ammonia by cytochrome c nitrite reductase

High-resolution structural analysis of a novel octaheme cytochrome c nitrite reductase from the haloalkaliphilic bacterium Thioalkalivibrio nitratireducens

Structural studies of hydroxylamine oxidoreductase reveal a unique heme cofactor and a previously unidentified interaction partner

The 2.8 A structure of hydroxylamine oxidoreductase from a nitrifying chemoautotrophic bacterium, Nitrosomonas europaea

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