Magnetic circular dichroism studies of the active site structure of hemoprotein H-450: Comparison to cytochrome P-450 and sensitivity of pH effects

Biochemical and Biophysical Research Communications

Volumn 165, Issue 3, 1989, Pages 1170-1176

  Svastits, Edmund W ^a   Alberta, John A ^a   Kim, In Cheol ^b   Dawson, John H ^a  

^a UNIVERSITY OF SOUTH CAROLINA   (United States)

^b UNIVERSITY OF NEW MEXICO SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME P450; HEMOPROTEIN;

ANIMAL CELL; ARTICLE; LIVER; NONHUMAN; PRIORITY JOURNAL; RAT;

ANIMAL; BINDING SITES; CAMPHOR 5-MONOOXYGENASE; CARBON MONOXIDE; CIRCULAR DICHROISM; COMPARATIVE STUDY; CYTOCHROME P-450 ENZYME SYSTEM; FERRIC COMPOUNDS; FERROUS COMPOUNDS; HEMATOPORPHYRINS; HYDROGEN-ION CONCENTRATION; LIVER; MIXED FUNCTION OXYGENASES; RATS; SPECTRUM ANALYSIS; SUPPORT, NON-U.S. GOV'T; SUPPORT, U.S. GOV'T, P.H.S.;

ANIMALIA;

EID: 0024792391     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/0006-291X(89)92725-3     Document Type: Article

References (19)