Crystal structure of heme oxygenase from the gram-negative pathogen Neisseria meningitidis and a comparison with mammalian heme oxygenase-1
about
Involvement of NADPH in the interaction between heme oxygenase-1 and cytochrome P450 reductaseComparison of apo- and heme-bound crystal structures of a truncated human heme oxygenase-2Crystal structure of rat heme oxygenase-1 in complex with heme bound to azide. Implication for regiospecific hydroxylation of heme at the alpha-meso carbonComparison of the heme-free and -bound crystal structures of human heme oxygenase-1Crystal structure of rat heme oxygenase-1 in complex with biliverdin-iron chelate. Conformational change of the distal helix during the heme cleavage reactionCrystal structures of the NO- and CO-bound heme oxygenase from Neisseriae meningitidis. Implications for O2 activationThe crystal structures of the ferric and ferrous forms of the heme complex of HmuO, a heme oxygenase of Corynebacterium diphtheriaeCrystal structure of the dioxygen-bound heme oxygenase from Corynebacterium diphtheriae: implications for heme oxygenase functionCrystallographic and Spectroscopic Insights into Heme Degradation by Mycobacterium tuberculosis MhuDUnusual Diheme Conformation of the Heme-Degrading Protein from Mycobacterium tuberculosisThe IsdG-family of haem oxygenases degrades haem to a novel chromophoreCrystal Structure and Biochemical Features of EfeB/YcdB from Escherichia coli O157Regulation of intracellular heme levels by HMX1, a homologue of heme oxygenase, in Saccharomyces cerevisiae.Metabolic flux of extracellular heme uptake in Pseudomonas aeruginosa is driven by the iron-regulated heme oxygenase (HemO)Solution 1H NMR investigation of the active site molecular and electronic structures of substrate-bound, cyanide-inhibited HmuO, a bacterial heme oxygenase from Corynebacterium diphtheriae.1H NMR investigation of the solution structure of substrate-free human heme oxygenase: comparison to the cyanide-inhibited, substrate-bound complex.Modulation of the axial water hydrogen-bonding properties by chemical modification of the substrate in resting state, substrate-bound heme oxygenase from Neisseria meningitidis; coupling to the distal H-bond network via ordered water molecules.Characterization of the spontaneous "aging" of the heme oxygenase from the pathological bacterium Neisseria meningitidis via cleavage of the C-terminus in contact with the substrate. Implications for functional studies and the crystal structure.1H NMR study of the magnetic properties and electronic structure of the hydroxide complex of substrate-bound heme oxygenase from Neisseria meningitidis: influence of the axial water deprotonation on the distal H-bond network.Diatomic ligand discrimination by the heme oxygenases from Neisseria meningitidis and Pseudomonas aeruginosa.Electronic properties of the highly ruffled heme bound to the heme degrading enzyme IsdI.Identification of an Escherichia coli O157:H7 heme oxygenase with tandem functional repeatsInduced fit on heme binding to the Pseudomonas aeruginosa cytoplasmic protein (PhuS) drives interaction with heme oxygenase (HemO)Bacillus anthracis IsdG, a heme-degrading monooxygenaseHeme enzyme structure and function.HutZ is required for efficient heme utilization in Vibrio choleraeThe hmuQ and hmuD genes from Bradyrhizobium japonicum encode heme-degrading enzymes.The Escherichia coli protein YfeX functions as a porphyrinogen oxidase, not a heme dechelataseInfluence of substrate modification and C-terminal truncation on the active site structure of substrate-bound heme oxygenase from Neisseriae meningitidis. A 1H NMR study.Iron transport systems in Neisseria meningitidisRole of propionates in substrate binding to heme oxygenase from Neisseria meningitidis: a nuclear magnetic resonance study1H NMR study of the effect of variable ligand on heme oxygenase electronic and molecular structure.Structures of the substrate-free and product-bound forms of HmuO, a heme oxygenase from corynebacterium diphtheriae: x-ray crystallography and molecular dynamics investigation.On the pathways of biologically relevant diatomic gases through proteins. Dioxygen and heme oxygenase from the perspective of molecular dynamics.Homologues of neisserial heme oxygenase in gram-negative bacteria: degradation of heme by the product of the pigA gene of Pseudomonas aeruginosaMetabolite-driven Regulation of Heme Uptake by the Biliverdin IXβ/δ-Selective Heme Oxygenase (HemO) of Pseudomonas aeruginosa.Function Coupling Mechanism of PhuS and HemO in Heme Degradation.Structural and mutational analyses of the Leptospira interrogans virulence-related heme oxygenase provide insights into its catalytic mechanism.Heme utilization by pathogenic bacteria: not all pathways lead to biliverdin.Crystal structure of heme oxygenase-1 from cyanobacterium Synechocystis sp. PCC 6803 in complex with heme.
P2860
Q24310223-6E6DAA15-6AAB-4B56-8095-C5100D82EDDFQ24621015-D3DB4813-32C2-4EB0-91BC-AFE3828373CCQ27639657-F603E91A-AE5F-48BB-A392-296C52C92763Q27640232-931A4B3F-1EA4-44D1-BC6A-4A534C188E8AQ27641404-D9003279-E229-42E6-8B83-5A923E876801Q27641460-C4FA6E5E-B56C-4B28-AE3C-697C0D60EB07Q27642658-0394797D-3FA8-44BB-8D5F-1EE01612E111Q27643141-DF5799C9-DC19-4FAD-8178-0BE03D79DBE9Q27644563-CB50D47F-201A-4AB5-A9F0-2E9EB3D6FD5EQ27658200-6A7F5CC0-6CDA-4640-9ED6-24C26D96002DQ27660036-90109A49-CAAA-4C73-9A84-728D38654CF4Q27666975-A5FA1ADF-35F1-4C21-BABF-9269D5F7E362Q27939241-5B275001-6395-42FD-A61E-44F9E8790FD9Q28492849-F7E2CC37-7343-4DC1-84D2-E9E971CF8F73Q30754996-7F16C865-10BA-4B99-9957-F68EC1F4D1E8Q30885667-768212B7-FBD1-4286-ABDE-590D0F666015Q31039839-77B468FF-326C-4EAA-8DD4-210A5B9CAE21Q33237045-3DCE636B-F5DC-4AD5-860E-A31AC2BF3977Q33243618-3A4219E8-69FD-4EA1-8D5D-E177D312C760Q33263176-41D7C05D-C0F6-4EDA-9A49-583A7E4D5AEDQ33970868-FE36D4E7-5BB8-4B7F-ABB3-EE33CA81A15CQ34144548-77E6447F-D7C3-4B4E-9487-A68E13A8D829Q34209000-AA5EDAB1-9CF1-4DC3-9653-F993ABA42C3AQ34303390-EA1702E8-5C30-48E5-8F1C-344E0AAADD9BQ34396417-66EDBB9F-B2BA-433B-A232-E76DB60AE1D6Q34435039-11F34F1F-EE7E-4F32-A856-86C85C4B586FQ35075596-99D0F179-2C62-4ACC-913E-49B29B27439CQ35547977-1F8F23A2-2018-4000-8A10-EEC4331DD6E6Q35648424-E6C94BB3-A853-4C0B-BE4B-108B21C828E2Q35684980-C625FFB3-A1D2-46F3-803F-E4D49152C881Q36445749-8EE112E2-4627-453F-9BA1-8986B5016032Q37298678-2AE5905D-8614-4192-A095-1F4030FA2C73Q37348889-F1D14D04-0CD3-4B23-855F-9DF9B5D56BBEQ39436699-5C5544D3-4A79-4966-8939-854961538D99Q39529862-0AE80300-4801-4A23-956B-CA3E52FAD231Q41161702-9FCD11AA-B780-43AC-87F5-7C6D14E1DE05Q41193258-F9511102-68CB-4708-AA5D-7DF208734B5EQ41237558-E1189F54-4B28-496E-A250-5A3172CE5840Q41991304-E38B0048-224B-4987-B12F-A1CAB90C82B4Q42641232-732BF699-144F-4616-945F-69CC514A7860
P2860
Crystal structure of heme oxygenase from the gram-negative pathogen Neisseria meningitidis and a comparison with mammalian heme oxygenase-1
description
2001 nî lūn-bûn
@nan
2001 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Crystal structure of heme oxyg ...... ith mammalian heme oxygenase-1
@ast
Crystal structure of heme oxyg ...... ith mammalian heme oxygenase-1
@en
Crystal structure of heme oxyg ...... ith mammalian heme oxygenase-1
@nl
type
label
Crystal structure of heme oxyg ...... ith mammalian heme oxygenase-1
@ast
Crystal structure of heme oxyg ...... ith mammalian heme oxygenase-1
@en
Crystal structure of heme oxyg ...... ith mammalian heme oxygenase-1
@nl
prefLabel
Crystal structure of heme oxyg ...... ith mammalian heme oxygenase-1
@ast
Crystal structure of heme oxyg ...... ith mammalian heme oxygenase-1
@en
Crystal structure of heme oxyg ...... ith mammalian heme oxygenase-1
@nl
P2093
P921
P356
P1433
P1476
Crystal structure of heme oxyg ...... ith mammalian heme oxygenase-1
@en
P2093
P304
P356
10.1021/BI0110239
P407
P577
2001-09-25T00:00:00Z