Neutral thiol as a proximal ligand to ferrous heme iron: Implications for heme proteins that lose cysteine thiolate ligation on reduction

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

Volumn 100, Issue 7, 2003, Pages 3641-3646

  Perera, Roshan ^a   Sono, Masanori ^a   Sigman, Jeffrey A ^c   Pfister, Thomas D ^c   Lut, Yi ^c   Dawson, John H ^a,b  

^a UNIVERSITY OF SOUTH CAROLINA   (United States)

^b UNIVERSITY OF SOUTH CAROLINA SCHOOL OF MEDICINE   (United States)

^c UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; CYSTEINE THIOLATE; CYTOCHROME C PEROXIDASE; CYTOCHROME P420; CYTOCHROME P450; FERROUS ION; HEME IRON; HEMOPROTEIN; MYOGLOBIN; NITROUS OXIDE; OXYGEN; OXYGEN DERIVATIVE; SULFIDE; SULFUR DERIVATIVE; THIOL DERIVATIVE; UNCLASSIFIED DRUG; CYTOCHROME C OXIDASE;

ARTICLE; CIRCULAR DICHROISM; GENE MUTATION; IRON METABOLISM; LIGAND BINDING; LIGATION; LIVER MICROSOME; MAGNETISM; METAL BINDING; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTON TRANSPORT; PSEUDOMONAS AERUGINOSA; REDUCTION; SPECTROSCOPY; CHEMISTRY; GENETICS; METABOLISM; OXIDATION REDUCTION REACTION; PROTEIN BINDING; PROTEIN CONFORMATION; SPECTROPHOTOMETRY;

PSEUDOMONAS; PSEUDOMONAS AERUGINOSA;

CIRCULAR DICHROISM; CYSTEINE; CYTOCHROME-C PEROXIDASE; ELECTRON TRANSPORT COMPLEX IV; HEMEPROTEINS; MYOGLOBIN; OXIDATION-REDUCTION; OXYGEN; PROTEIN BINDING; PROTEIN CONFORMATION; SPECTROPHOTOMETRY; SULFHYDRYL COMPOUNDS;

EID: 0037390012     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0737142100     Document Type: Article

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