Crystallographic Trapping of Heme Loss Intermediates during the Nitrite-Induced Degradation of Human Hemoglobin - Wikidata - awgldk - TriplyDB

Crystallographic Trapping of Heme Loss Intermediates during the Nitrite-Induced Degradation of Human Hemoglobin

Crystallographic Trapping of Heme Loss Intermediates during the Nitrite-Induced Degradation of Human Hemoglobin

http://www.wikidata.org/entity/Q27671930

about

Unveiling the three-dimensional structure of the green pigment of nitrite-cured meat Crystallographic characterization of the nitric oxide derivative of R-state human hemoglobin Degradation of human hemoglobin by organic C-nitroso compounds Leghemoglobin green derivatives with nitrated hemes evidence production of highly reactive nitrogen species during aging of legume nodules Reactivity of the human hemoglobin "dark side".Integrative and comparative reproductive biology: From alligators to xenobiotics.Resonance Raman detection of the myoglobin nitrito heme Fe-O-N=O/2-nitrovinyl species: implications for helix E-helix F interactions.

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P2860

Crystallographic Trapping of Heme Loss Intermediates during the Nitrite-Induced Degradation of Human Hemoglobin

http://www.wikidata.org/entity/Q27671930

description

2011 nî lūn-bûn

@nan

2011 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի հոտեմբերին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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Crystallographic Trapping of H ...... egradation of Human Hemoglobin

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Crystallographic Trapping of H ...... egradation of Human Hemoglobin

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Faik N Musayev

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George B Richter-Addo

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Jun Yi

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Leonard M Thomas

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Martin K Safo

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P2860

A pH-dependent aquomet-to-hemichrome transition in crystalline horse methemoglobin

The nitrite anion binds to human hemoglobin via the uncommon O-nitrito mode

Structure of human R-state aquomethemoglobin at 2.0 Å resolution

His64(E7)-->Tyr apomyoglobin as a reagent for measuring rates of hemin dissociation

Coot: model-building tools for molecular graphics

The finer things in X-ray diffraction data collection

Refinement of macromolecular structures by the maximum-likelihood method

PHENIX: building new software for automated crystallographic structure determination

The Molecular Mechanism of Autoxidation for Myoglobin and Hemoglobin: A Venerable Puzzle.

Unstable hemoglobins: the role of heme loss in Heinz body formation

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scholarly article

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10.1021/BI2009322

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39

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