Flavodoxin hydroquinone reduces Azotobacter vinelandii Fe protein to the all-ferrous redox state with a S = 0 spin state

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

Volumn 103, Issue 46, 2006, Pages 17131-17136

  Lowery, Thomas J ^a   Wilson, Phillip E ^b   Zhang, Bo ^b   Bunker, Jared ^a   Harrison, Roger G ^b   Nyborg, Andrew C ^b   Thiriot, David ^b   Watt, Gerald D ^b  

^a BRIGHAM YOUNG UNIVERSITY   (United States)

^b Brigham Young University   (United States)

Author keywords

All ferrous cluster; Nitrogenase

Indexed keywords

FLAVODOXIN; FLAVODOXIN HYDROQUINONE; HYDROQUINONE; IRON SULFUR PROTEIN; MOLYBDENUM IRON PROTEIN; NITROGEN; NITROGENASE; UNCLASSIFIED DRUG;

ARTICLE; AZOTOBACTER VINELANDII; CATALYSIS; ELECTRON SPIN RESONANCE; ENZYME ACTIVITY; MOSSBAUER SPECTROSCOPY; NITROGEN FIXATION; NITROGEN METABOLISM; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; ULTRAVIOLET SPECTROSCOPY;

AZOTOBACTER VINELANDII; FLAVODOXIN; HYDROQUINONES; IRON; MAGNETIC RESONANCE SPECTROSCOPY; NUCLEOTIDES; OXIDATION-REDUCTION; OXIDOREDUCTASES; OXYGEN; SULFUR;

AZOTOBACTER VINELANDII;

EID: 33751217465     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0603223103     Document Type: Article

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