Characterization of the siroheme active site in spinach nitrite reductase by resonance Raman spectroscopy. 1985

M R Ondrias, and S D Carson, and M Hirasawa, and D B Knaff

The resonance Raman spectra of various species of spinach nitrite reductase (ferredoxin: nitrite oxidoreductase, EC 1.7.7.1) have been obtained with Soret excitation. These spectra allow for the vibrational properties of the unique siroheme chromophore at the enzyme's active site. The wholesale reordering of siroheme vibrational properties relative to those of protoporphyrins can be rationalized as resulting from a combination of symmetry lowering and bond order reductions within the siroheme macrocyle.

UI MeSH Term Description Entries
D009247 NADH, NADPH Oxidoreductases A group of oxidoreductases that act on NADH or NADPH. In general, enzymes using NADH or NADPH to reduce a substrate are classified according to the reverse reaction, in which NAD+ or NADP+ is formally regarded as an acceptor. This subclass includes only those enzymes in which some other redox carrier is the acceptor. (Enzyme Nomenclature, 1992, p100) EC 1.6. Oxidoreductases, NADH, NADPH,NADPH Oxidoreductases NADH,Oxidoreductases NADH, NADPH
D009572 Nitrite Reductases A group of enzymes that oxidize diverse nitrogenous substances to yield nitrite. (Enzyme Nomenclature, 1992) EC 1. Nitrite Reductase,Reductase, Nitrite,Reductases, Nitrite
D010944 Plants Multicellular, eukaryotic life forms of kingdom Plantae. Plants acquired chloroplasts by direct endosymbiosis of CYANOBACTERIA. They are characterized by a mainly photosynthetic mode of nutrition; essentially unlimited growth at localized regions of cell divisions (MERISTEMS); cellulose within cells providing rigidity; the absence of organs of locomotion; absence of nervous and sensory systems; and an alternation of haploid and diploid generations. It is a non-taxonomical term most often referring to LAND PLANTS. In broad sense it includes RHODOPHYTA and GLAUCOPHYTA along with VIRIDIPLANTAE. Plant
D006418 Heme The color-furnishing portion of hemoglobin. It is found free in tissues and as the prosthetic group in many hemeproteins. Ferroprotoporphyrin,Protoheme,Haem,Heme b,Protoheme IX
D001665 Binding Sites The parts of a macromolecule that directly participate in its specific combination with another molecule. Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining
D013059 Spectrum Analysis, Raman Analysis of the intensity of Raman scattering of monochromatic light as a function of frequency of the scattered light. Raman Spectroscopy,Analysis, Raman Spectrum,Raman Optical Activity Spectroscopy,Raman Scattering,Raman Spectrum Analysis,Scattering, Raman,Spectroscopy, Raman

Related Publications

M R Ondrias, and S D Carson, and M Hirasawa, and D B Knaff
November 1989, Archives of biochemistry and biophysics,
M R Ondrias, and S D Carson, and M Hirasawa, and D B Knaff
March 1993, The Journal of biological chemistry,
M R Ondrias, and S D Carson, and M Hirasawa, and D B Knaff
July 1975, Archives of biochemistry and biophysics,
M R Ondrias, and S D Carson, and M Hirasawa, and D B Knaff
March 1995, Biochemistry,
M R Ondrias, and S D Carson, and M Hirasawa, and D B Knaff
February 1977, The Journal of biological chemistry,
M R Ondrias, and S D Carson, and M Hirasawa, and D B Knaff
November 1991, Archives of biochemistry and biophysics,
M R Ondrias, and S D Carson, and M Hirasawa, and D B Knaff
October 1995, Archives of biochemistry and biophysics,
M R Ondrias, and S D Carson, and M Hirasawa, and D B Knaff
July 1977, Biochemical and biophysical research communications,
M R Ondrias, and S D Carson, and M Hirasawa, and D B Knaff
September 1993, Biochemistry,
Copied contents to your clipboard!