Connecting nitrogenase intermediates with the kinetic scheme for N 2 reduction by a relaxation protocol and identification of the N 2 binding state

Proceedings of the National Academy of Sciences of the United States of America

Volumn 104, Issue 5, 2007, Pages 1451-1455

  Lukoyanov, Dmitriy ^c   Barney, Brett M ^a   Dean, Dennis R ^b   Seefeldt, Lance C ^a   Hoffman, Brian M ^c  

^a UTAH STATE UNIVERSITY   (United States)

^b VIRGINIA POLYTECHNIC INSTITUTE AND STATE UNIVERSITY   (United States)

^c NORTHWESTERN UNIVERSITY   (United States)

Author keywords

Intermediate; Kinetic isotope effect

Indexed keywords

IRON; ISOTOPE; MOLYBDENUM; NITROGEN; NITROGENASE;

ARTICLE; BINDING SITE; ELECTRON TRANSPORT; ENZYME ACTIVE SITE; ENZYME SUBSTRATE; KINETICS; NITROGEN METABOLISM; NONHUMAN; PRIORITY JOURNAL; REDUCTION;

AZOTOBACTER VINELANDII; BIOCHEMISTRY; ELECTRON SPIN RESONANCE SPECTROSCOPY; ELECTRONS; HYDROGEN-ION CONCENTRATION; KINETICS; MODELS, CHEMICAL; MOLYBDOFERREDOXIN; NITROGEN; NITROGENASE; PROTEIN BINDING; PROTONS; SUBSTRATE SPECIFICITY;

EID: 33846781675     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0610975104     Document Type: Article

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