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Journal Abstract Search

136 related items for PubMed ID: 22001779

  • 1. Molecular structure and function of bacterial nitric oxide reductase.
    Hino T, Nagano S, Sugimoto H, Tosha T, Shiro Y.
    Biochim Biophys Acta; 2012 Apr; 1817(4):680-7. PubMed ID: 22001779
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  • 2. Structures of reduced and ligand-bound nitric oxide reductase provide insights into functional differences in respiratory enzymes.
    Sato N, Ishii S, Sugimoto H, Hino T, Fukumori Y, Sako Y, Shiro Y, Tosha T.
    Proteins; 2014 Jul; 82(7):1258-71. PubMed ID: 24338896
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  • 7. Characterization of quinol-dependent nitric oxide reductase from Geobacillus stearothermophilus: enzymatic activity and active site structure.
    Terasaka E, Okada N, Sato N, Sako Y, Shiro Y, Tosha T.
    Biochim Biophys Acta; 2014 Jul; 1837(7):1019-26. PubMed ID: 24569054
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  • 8. Low-spin heme b(3) in the catalytic center of nitric oxide reductase from Pseudomonas nautica.
    Timóteo CG, Pereira AS, Martins CE, Naik SG, Duarte AG, Moura JJ, Tavares P, Huynh BH, Moura I.
    Biochemistry; 2011 May 24; 50(20):4251-62. PubMed ID: 21452843
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  • 10. Structure and function of bacterial nitric oxide reductases: nitric oxide reductase, anaerobic enzymes.
    Shiro Y.
    Biochim Biophys Acta; 2012 Oct 24; 1817(10):1907-13. PubMed ID: 22425814
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  • 11. Biochemistry. Catalyzing NO to N2O in the nitrogen cycle.
    Moënne-Loccoz P, Fee JA.
    Science; 2010 Dec 17; 330(6011):1632-3. PubMed ID: 21164002
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  • 14. Bacterial denitrifying nitric oxide reductases and aerobic respiratory terminal oxidases use similar delivery pathways for their molecular substrates.
    Mahinthichaichan P, Gennis RB, Tajkhorshid E.
    Biochim Biophys Acta Bioenerg; 2018 Sep 17; 1859(9):712-724. PubMed ID: 29883591
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  • 16. Active-site models of bacterial nitric oxide reductase featuring tris-histidyl and glutamic acid mimics: influence of a carboxylate ligand on Fe(B) binding and the heme Fe/Fe(B) redox potential.
    Collman JP, Yan YL, Lei J, Dinolfo PH.
    Inorg Chem; 2006 Sep 18; 45(19):7581-3. PubMed ID: 16961346
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