Fourier transform infrared spectroscopy as a tool to study structural properties of cytochromes P450 (CYPs)

Analytical and Bioanalytical Chemistry

Volumn 392, Issue 6, 2008, Pages 1031-1058

  Jung, Christiane ^a,b  

^a MAX DELBRÜCK CENTER FOR MOLECULAR MEDICINE   (Germany)

^b KKS Ultraschall AG   (Switzerland)

Author keywords

Chloroperoxidase; CYP; Cytochrome P450; Fourier transform infrared spectroscopy; Nitric oxide synthase

Indexed keywords

ENZYMES; FOURIER TRANSFORM INFRARED SPECTROSCOPY; FOURIER TRANSFORMS; HEMOGLOBIN; NITRIC OXIDE; OXIDES; PORPHYRINS; PROTEINS; SPECTROSCOPIC ANALYSIS; SPECTRUM ANALYSIS;

ACTIVE COMPONENTS; CHLOROPEROXIDASE; CYP; CYTOCHROME P450; CYTOCHROMES P450; FOURIER TRANSFORM INFRARED; FTIR SPECTROSCOPIES; FUNCTION RELATIONSHIPS; HEME POCKETS; HEME PROTEINS; LIVING ORGANISMS; MECHANISTIC ASPECTS; METABOLIC PROCESSES; MONOOXYGENASE; PROTEIN INTERACTIONS; PROTEIN STRUCTURES; SECONDARY STRUCTURES; SPECIFIC PROPERTIES; STRUCTURE AND DYNAMICS; SUBSTRATE BINDS; SYNTHASE; THIOLATE;

INFRARED SPECTROSCOPY;

CHLORIDE PEROXIDASE; CYTOCHROME P450; HEMOPROTEIN; MIXED FUNCTION OXIDASE; NITRIC OXIDE SYNTHASE;

BINDING SITE; CATALYSIS; CHEMISTRY; ENZYME SPECIFICITY; HYDROXYLATION; INFRARED SPECTROSCOPY; METABOLISM; METHODOLOGY; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; REVIEW;

BINDING SITES; CATALYSIS; CHLORIDE PEROXIDASE; CYTOCHROME P-450 ENZYME SYSTEM; HEMEPROTEINS; HYDROXYLATION; MIXED FUNCTION OXYGENASES; NITRIC OXIDE SYNTHASE; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; SUBSTRATE SPECIFICITY;

EID: 54949084248     PISSN: 16182642     EISSN: 16182650     Source Type: Journal    
DOI: 10.1007/s00216-008-2216-4     Document Type: Review

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