1H-NMR study of reduced heme proteins myoglobin and cytochrome P450. 1993

L Banci, and I Bertini, and S Marconi, and R Pierattelli
Department of Chemistry, University of Florence, Italy.

The 1H-NMR spectra of deoxymyoglobin and reduced cytochrome P450 are analyzed by NOE spectroscopy. Progress has been made in the assignment of the hyperfine-shifted signals of deoxymyoglobin. The nuclear longitudinal-relaxation-time values indicate short electron-relaxation times whereas Curie relaxation contributes significantly to the signals linewidths. For reduced cytochrome P450 the linewidths are larger due to the Curie-relaxation contribution in a large protein. Therefore, the spectral information is poor. The electron-relaxation rates are discussed in terms of possible electronic structure.

UI MeSH Term Description Entries
D008297 Male Males
D009211 Myoglobin A conjugated protein which is the oxygen-transporting pigment of muscle. It is made up of one globin polypeptide chain and one heme group.
D009682 Magnetic Resonance Spectroscopy Spectroscopic method of measuring the magnetic moment of elementary particles such as atomic nuclei, protons or electrons. It is employed in clinical applications such as NMR Tomography (MAGNETIC RESONANCE IMAGING). In Vivo NMR Spectroscopy,MR Spectroscopy,Magnetic Resonance,NMR Spectroscopy,NMR Spectroscopy, In Vivo,Nuclear Magnetic Resonance,Spectroscopy, Magnetic Resonance,Spectroscopy, NMR,Spectroscopy, Nuclear Magnetic Resonance,Magnetic Resonance Spectroscopies,Magnetic Resonance, Nuclear,NMR Spectroscopies,Resonance Spectroscopy, Magnetic,Resonance, Magnetic,Resonance, Nuclear Magnetic,Spectroscopies, NMR,Spectroscopy, MR
D010084 Oxidation-Reduction A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471). Redox,Oxidation Reduction
D003577 Cytochrome P-450 Enzyme System A superfamily of hundreds of closely related HEMEPROTEINS found throughout the phylogenetic spectrum, from animals, plants, fungi, to bacteria. They include numerous complex monooxygenases (MIXED FUNCTION OXYGENASES). In animals, these P-450 enzymes serve two major functions: (1) biosynthesis of steroids, fatty acids, and bile acids; (2) metabolism of endogenous and a wide variety of exogenous substrates, such as toxins and drugs (BIOTRANSFORMATION). They are classified, according to their sequence similarities rather than functions, into CYP gene families (>40% homology) and subfamilies (>59% homology). For example, enzymes from the CYP1, CYP2, and CYP3 gene families are responsible for most drug metabolism. Cytochrome P-450,Cytochrome P-450 Enzyme,Cytochrome P-450-Dependent Monooxygenase,P-450 Enzyme,P450 Enzyme,CYP450 Family,CYP450 Superfamily,Cytochrome P-450 Enzymes,Cytochrome P-450 Families,Cytochrome P-450 Monooxygenase,Cytochrome P-450 Oxygenase,Cytochrome P-450 Superfamily,Cytochrome P450,Cytochrome P450 Superfamily,Cytochrome p450 Families,P-450 Enzymes,P450 Enzymes,Cytochrome P 450,Cytochrome P 450 Dependent Monooxygenase,Cytochrome P 450 Enzyme,Cytochrome P 450 Enzyme System,Cytochrome P 450 Enzymes,Cytochrome P 450 Families,Cytochrome P 450 Monooxygenase,Cytochrome P 450 Oxygenase,Cytochrome P 450 Superfamily,Enzyme, Cytochrome P-450,Enzyme, P-450,Enzyme, P450,Enzymes, Cytochrome P-450,Enzymes, P-450,Enzymes, P450,Monooxygenase, Cytochrome P-450,Monooxygenase, Cytochrome P-450-Dependent,P 450 Enzyme,P 450 Enzymes,P-450 Enzyme, Cytochrome,P-450 Enzymes, Cytochrome,Superfamily, CYP450,Superfamily, Cytochrome P-450,Superfamily, Cytochrome P450
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D014907 Whales Large marine mammals of the order CETACEA. In the past, they were commercially valued for whale oil, for their flesh as human food and in ANIMAL FEED and FERTILIZERS, and for baleen. Today, there is a moratorium on most commercial whaling, as all species are either listed as endangered or threatened. Beaked Whales,Berardius,Caperea,Dwarf Sperm Whale,Giant Bottle-Nosed Whales,Goose-Beaked Whale,Gray Whale,Mesoplodon,Narwhals,Pygmy Right Whale,Pygmy Sperm Whale,Right Whale, North Atlantic,Right Whale, Southern,Ziphiidae,Ziphius,Eschrichtius robustus,Eubalaena australis,Grey Whale,Monodon monoceros,North Atlantic Right Whale,Beaked Whale,Bottle-Nosed Whale, Giant,Bottle-Nosed Whales, Giant,Dwarf Sperm Whales,Giant Bottle Nosed Whales,Giant Bottle-Nosed Whale,Goose Beaked Whale,Goose-Beaked Whales,Gray Whales,Grey Whales,Narwhal,Pygmy Right Whales,Pygmy Sperm Whales,Right Whale, Pygmy,Right Whales, Pygmy,Right Whales, Southern,Southern Right Whale,Southern Right Whales,Sperm Whale, Dwarf,Sperm Whale, Pygmy,Sperm Whales, Dwarf,Sperm Whales, Pygmy,Whale,Whale, Grey,Whale, Southern Right,Whales, Grey,Whales, Southern Right
D016958 Pseudomonas putida A species of gram-negative, aerobic bacteria isolated from soil and water as well as clinical specimens. Occasionally it is an opportunistic pathogen.

Related Publications

L Banci, and I Bertini, and S Marconi, and R Pierattelli
June 1991, European journal of biochemistry,
L Banci, and I Bertini, and S Marconi, and R Pierattelli
February 2003, Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry,
L Banci, and I Bertini, and S Marconi, and R Pierattelli
September 1998, Inorganic chemistry,
L Banci, and I Bertini, and S Marconi, and R Pierattelli
May 1990, European journal of biochemistry,
L Banci, and I Bertini, and S Marconi, and R Pierattelli
October 2011, Biotechnology letters,
L Banci, and I Bertini, and S Marconi, and R Pierattelli
January 1996, Life sciences,
L Banci, and I Bertini, and S Marconi, and R Pierattelli
May 2019, Journal of inorganic biochemistry,
L Banci, and I Bertini, and S Marconi, and R Pierattelli
November 1998, Biochimica et biophysica acta,
L Banci, and I Bertini, and S Marconi, and R Pierattelli
November 1990, Biochimica et biophysica acta,
Copied contents to your clipboard!