| scholarly article | Q13442814 |
| P2093 | author name string | Kei Wada | |
| Keiichi Fukuyama | |||
| Masakazu Sugishima | |||
| P2860 | cites work | Heme catabolism by the reconstituted heme oxygenase system | Q67531412 |
| Purification and characterization of human biliverdin reductase | Q70539873 | ||
| Purification and characterization of biliverdin reductase from rat liver | Q70729972 | ||
| Oxygenated form of heme . heme oxygenase complex and requirement for second electron to initiate heme degradation from the oxygenated complex | Q71848214 | ||
| Zinc . protoporphyrin is a selective inhibitor of heme oxygenase activity in the neonatal rat | Q71853431 | ||
| Resonance Raman and EPR spectroscopic studies on heme-heme oxygenase complexes | Q72655657 | ||
| Heme-heme oxygenase complex. Structure of the catalytic site and its implication for oxygen activation | Q72724906 | ||
| Crystallization and preliminary X-ray diffraction analysis of a rat biliverdin reductase | Q74219973 | ||
| Crystallization and preliminary X-ray diffraction studies on the water soluble form of rat heme oxygenase-1 in complex with heme | Q77360202 | ||
| Ferric alpha-hydroxyheme bound to heme oxygenase can be converted to verdoheme by dioxygen in the absence of added reducing equivalents | Q77895409 | ||
| Imidazole-dioxolane compounds as isozyme-selective heme oxygenase inhibitors | Q79842136 | ||
| Reduction of oxaporphyrin ring of CO-bound α-verdoheme complexed with heme oxygenase-1 by NADPH-cytochrome P450 reductase | Q83075264 | ||
| Disruption of an active site hydrogen bond converts human heme oxygenase-1 into a peroxidase | Q95717606 | ||
| Heme oxygenase and heme degradation | Q21710702 | ||
| Expression and characterization of full-length human heme oxygenase-1: the presence of intact membrane-binding region leads to increased binding affinity for NADPH cytochrome P450 reductase | Q24296465 | ||
| Involvement of NADPH in the interaction between heme oxygenase-1 and cytochrome P450 reductase | Q24310223 | ||
| Oligomerization is crucial for the stability and function of heme oxygenase-1 in the endoplasmic reticulum | Q24339396 | ||
| Biliverdin reductase: a major physiologic cytoprotectant | Q24541497 | ||
| Comparison of apo- and heme-bound crystal structures of a truncated human heme oxygenase-2 | Q24621015 | ||
| Three-dimensional structure of NADPH-cytochrome P450 reductase: prototype for FMN- and FAD-containing enzymes | Q24654975 | ||
| Crystal structure of rat heme oxygenase-1 in complex with heme | Q27622187 | ||
| Crystal structure of rat biliverdin reductase | Q27630105 | ||
| Crystal structure of heme oxygenase from the gram-negative pathogen Neisseria meningitidis and a comparison with mammalian heme oxygenase-1 | Q27634857 | ||
| Crystal structure of rat apo-heme oxygenase-1 (HO-1): mechanism of heme binding in HO-1 inferred from structural comparison of the apo and heme complex forms | Q27639069 | ||
| Crystal structure of a biliverdin IXalpha reductase enzyme-cofactor complex | Q27639221 | ||
| Crystal structure of rat heme oxygenase-1 in complex with heme bound to azide. Implication for regiospecific hydroxylation of heme at the alpha-meso carbon | Q27639657 | ||
| Comparison of the heme-free and -bound crystal structures of human heme oxygenase-1 | Q27640232 | ||
| Crystal structure of rat heme oxygenase-1 in complex with biliverdin-iron chelate. Conformational change of the distal helix during the heme cleavage reaction | Q27641404 | ||
| Crystal structures of ferrous and CO-, CN(-)-, and NO-bound forms of rat heme oxygenase-1 (HO-1) in complex with heme: structural implications for discrimination between CO and O2 in HO-1 | Q27641850 | ||
| The crystal structures of the ferric and ferrous forms of the heme complex of HmuO, a heme oxygenase of Corynebacterium diphtheriae | Q27642658 | ||
| Crystal structure of the dioxygen-bound heme oxygenase from Corynebacterium diphtheriae: implications for heme oxygenase function | Q27643141 | ||
| X-ray crystallographic and biochemical characterization of the inhibitory action of an imidazole-dioxolane compound on heme oxygenase | Q27643656 | ||
| X-ray crystal structure of human heme oxygenase-1 in complex with 1-(adamantan-1-yl)-2-(1H-imidazol-1-yl)ethanone: a common binding mode for imidazole-based heme oxygenase-1 inhibitors | Q27652197 | ||
| Structure and Function of an NADPH-Cytochrome P450 Oxidoreductase in an Open Conformation Capable of Reducing Cytochrome P450 | Q27653521 | ||
| X-ray crystal structure of human heme oxygenase-1 with (2R,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4[((5-trifluoromethylpyridin-2-yl)thio)methyl]-1,3-dioxolane: a novel, inducible binding mode | Q27656400 | ||
| Dioxygen activation for the self-degradation of heme: reaction mechanism and regulation of heme oxygenase | Q27660464 | ||
| Conformational Changes of NADPH-Cytochrome P450 Oxidoreductase Are Essential for Catalysis and Cofactor Binding | Q27667024 | ||
| Discrimination between CO and O 2 in Heme Oxygenase: Comparison of Static Structures and Dynamic Conformation Changes following CO Photolysis | Q27674332 | ||
| A Novel, “Double-Clamp” Binding Mode for Human Heme Oxygenase-1 Inhibition | Q27676882 | ||
| Structural basis for the electron transfer from an open form of NADPH-cytochrome P450 oxidoreductase to heme oxygenase | Q27681796 | ||
| Distal regulation of heme binding of heme oxygenase-1 mediated by conformational fluctuations | Q27696835 | ||
| Rv2074 is a novel F420 H2 -dependent biliverdin reductase in Mycobacterium tuberculosis | Q27715540 | ||
| Human biliverdin reductase is a leucine zipper-like DNA-binding protein and functions in transcriptional activation of heme oxygenase-1 by oxidative stress | Q28214376 | ||
| Biliverdin reductase, a novel regulator for induction of activating transcription factor-2 and heme oxygenase-1 | Q28247218 | ||
| Biliverdin reductase: new features of an old enzyme and its potential therapeutic significance | Q28268811 | ||
| Bilirubin is an antioxidant of possible physiological importance | Q28288206 | ||
| The Arabidopsis HY2 gene encodes phytochromobilin synthase, a ferredoxin-dependent biliverdin reductase | Q28354306 | ||
| Coupled motions direct electrons along human microsomal P450 Chains | Q28478496 | ||
| The reactions of heme- and verdoheme-heme oxygenase-1 complexes with FMN-depleted NADPH-cytochrome P450 reductase. Electrons required for verdoheme oxidation can be transferred through a pathway not involving FMN | Q28566694 | ||
| Mass spectrometric identification of lysine residues of heme oxygenase-1 that are involved in its interaction with NADPH-cytochrome P450 reductase | Q28569380 | ||
| Mechanism of heme degradation by heme oxygenase | Q29397702 | ||
| Phytochrome structure and signaling mechanisms. | Q30486809 | ||
| Solution 1H NMR of the active site of substrate-bound, cyanide-inhibited human heme oxygenase. comparison to the crystal structure of the water-ligated form | Q30647375 | ||
| 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 | Q30754996 | ||
| Crystal structures of ferrous and ferrous-NO forms of verdoheme in a complex with human heme oxygenase-1: catalytic implications for heme cleavage | Q30975319 | ||
| CO-trapping site in heme oxygenase revealed by photolysis of its co-bound heme complex: mechanism of escaping from product inhibition. | Q31105739 | ||
| Nuclear localization of biliverdin reductase in the rat kidney: response to nephrotoxins that induce heme oxygenase-1. | Q31963580 | ||
| Diatomic ligand discrimination by the heme oxygenases from Neisseria meningitidis and Pseudomonas aeruginosa | Q33263176 | ||
| Function and distribution of bilin biosynthesis enzymes in photosynthetic organisms | Q33375085 | ||
| Human biliverdin reductase: a member of the insulin receptor substrate family with serine/threonine/tyrosine kinase activity | Q33771641 | ||
| The mechanism of heme oxygenase | Q33878368 | ||
| Hypoxic regulation of the cerebral microcirculation is mediated by a carbon monoxide-sensitive hydrogen sulfide pathway. | Q34122686 | ||
| NPAS2: a gas-responsive transcription factor | Q34160458 | ||
| Blue light and bilirubin excretion | Q34285422 | ||
| Structure and function of plant-type ferredoxins | Q34435668 | ||
| Heme oxygenase/carbon monoxide signaling pathways: regulation and functional significance | Q34773844 | ||
| Making light of it: the role of plant haem oxygenases in phytochrome chromophore synthesis | Q34797569 | ||
| Selectivity of imidazole-dioxolane compounds for in vitro inhibition of microsomal haem oxygenase isoforms | Q35545244 | ||
| Bacterial heme oxygenases | Q35877581 | ||
| Antioxidant activities of bile pigments | Q35877590 | ||
| Distinct phytochrome actions in nonvascular plants revealed by targeted inactivation of phytobilin biosynthesis | Q35991546 | ||
| Crystallization of recombinant human heme oxygenase-1. | Q36281120 | ||
| Role of cysteine residues in heme binding to human heme oxygenase-2 elucidated by two-dimensional NMR spectroscopy | Q36318748 | ||
| The enzymatic conversion of heme to bilirubin by microsomal heme oxygenase | Q36475899 | ||
| Structural insights into human heme oxygenase-1 inhibition by potent and selective azole-based compounds | Q36591335 | ||
| Structure and catalytic mechanism of heme oxygenase. | Q36834135 | ||
| Cyanobacteriochromes: a new superfamily of tetrapyrrole-binding photoreceptors in cyanobacteria | Q37291008 | ||
| Structures of the substrate-free and product-bound forms of HmuO, a heme oxygenase from corynebacterium diphtheriae: x-ray crystallography and molecular dynamics investigation | Q37348889 | ||
| Structural characterization of human heme oxygenase-1 in complex with azole-based inhibitors | Q37633749 | ||
| A substrate-bound structure of cyanobacterial biliverdin reductase identifies stacked substrates as critical for activity | Q37642479 | ||
| Crystallographic studies of heme oxygenase complexed with an unstable reaction intermediate, verdoheme. | Q38016674 | ||
| Overview of heme degradation pathway | Q38050386 | ||
| Measurement of membrane-bound human heme oxygenase-1 activity using a chemically defined assay system | Q38357560 | ||
| Purification and Properties of Biliverdin Reductases from Pig Spleen and Rat Liver1 | Q39282376 | ||
| Function and induction of the microsomal heme oxygenase | Q40158554 | ||
| Crystal structure of human heme oxygenase-1. | Q41687640 | ||
| Redox-linked domain movements in the catalytic cycle of cytochrome p450 reductase | Q41808959 | ||
| Expression, purification and preliminary X-ray crystallographic analysis of cyanobacterial biliverdin reductase | Q41839827 | ||
| Activation of biliverdin-IXalpha reductase by inorganic phosphate and related anions | Q41845888 | ||
| Crystal structure of heme oxygenase-1 from cyanobacterium Synechocystis sp. PCC 6803 in complex with heme | Q42641232 | ||
| Heme oxygenase reveals its strategy for catalyzing three successive oxygenation reactions | Q43261631 | ||
| Human biliverdin reductase is autophosphorylated, and phosphorylation is required for bilirubin formation | Q43559842 | ||
| A role for highly conserved carboxylate, aspartate-140, in oxygen activation and heme degradation by heme oxygenase-1. | Q43663150 | ||
| The reactivity of alpha-hydroxyhaem and verdohaem bound to haem oxygenase-1 to dioxygen and sodium dithionite | Q44188688 | ||
| Heme oxygenase in Candida albicans is regulated by hemoglobin and is necessary for metabolism of exogenous heme and hemoglobin to alpha-biliverdin | Q44654383 | ||
| Synthesis and evaluation of azalanstat analogues as heme oxygenase inhibitors | Q45266887 | ||
| Catalytic mechanism of heme oxygenase through EPR and ENDOR of cryoreduced oxy-heme oxygenase and its Asp 140 mutants | Q45712309 | ||
| Rat liver heme oxygenase. High level expression of a truncated soluble form and nature of the meso-hydroxylating species | Q46114677 | ||
| Expression and characterization of truncated human heme oxygenase (hHO-1) and a fusion protein of hHO-1 with human cytochrome P450 reductase | Q46138916 | ||
| Structural basis for novel delta-regioselective heme oxygenation in the opportunistic pathogen Pseudomonas aeruginosa | Q46184086 | ||
| Characterization of cyanobacterial biliverdin reductase. Conversion of biliverdin to bilirubin is important for normal phycobiliprotein biosynthesis | Q46185557 | ||
| Cystathionine beta-synthase as a carbon monoxide-sensitive regulator of bile excretion | Q46196479 | ||
| O(2)- and H(2)O(2)-dependent verdoheme degradation by heme oxygenase: reaction mechanisms and potential physiological roles of the dual pathway degradation. | Q46663766 | ||
| A kinetic study of the mechanism of conversion of alpha-hydroxyheme to verdoheme while bound to heme oxygenase. | Q46696382 | ||
| Microsomal heme oxygenase. Characterization of the enzyme | Q48959671 | ||
| Crystal structure of dimeric heme oxygenase-2 from Synechocystis sp. PCC 6803 in complex with heme. | Q50772239 | ||
| A heme oxygenase isoform is essential for aerobic growth in the cyanobacterium Synechocystis sp. PCC 6803: modes of differential operation of two isoforms/enzymes to adapt to low oxygen environments in cyanobacteria. | Q53226947 | ||
| Phytobilin biosynthesis: cloning and expression of a gene encoding soluble ferredoxin-dependent heme oxygenase from Synechocystis sp. PCC 6803. | Q53945955 | ||
| Biliverdin reductase of guinea pig liver. | Q55061450 | ||
| Detection of a Protein Conformational Equilibrium by Electrospray Ionisation-Ion Mobility-Mass Spectrometry | Q58571762 | ||
| The Oxygen and Carbon Monoxide Reactions of Heme Oxygenase | Q59599934 | ||
| P577 | publication date | 2018-12-17 | |
| P1433 | published in | Current Medicinal Chemistry | Q3007710 |
| P1476 | title | Recent Advances in the Understanding of the Reaction Chemistries of the Heme Catabolizing Enzymes HO and BVR Based on High Resolution Protein Structures |
| Q90444009 | Cardiac function dependence on carbon monoxide | cites work | P2860 |
Search more.