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.

No abstract is available for this paper.

• Publication year

  2006

• Venue

  Biochemistry

• Publication date

  2006-03-28

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1021/BI0523097PMID 16548515PMCID PMC2566967
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Heme oxygenase, steering dioxygen activation toward heme hydroxylation.

  2005cited by this paper
• Solution 1H NMR characterization of the distal H-bond network and the effective axial field in the resting-state, high-spin ferric, substrate-bound complex of heme oxygenase from N. meningitidis.

  2005cited by this paper
• Structural basis for novel delta-regioselective heme oxygenation in the opportunistic pathogen Pseudomonas aeruginosa.

  2004cited by this paper
• 1H NMR characterization of the solution active site structure of substrate-bound, cyanide-inhibited heme oxygenase from Neisseria meningitidis: comparison to crystal structures.

  2004cited by this paper
• The Crystal Structures of the Ferric and Ferrous Forms of the Heme Complex of HmuO, a Heme Oxygenase of Corynebacterium diphtheriae*

  2004cited by this paper
• Mixed regioselectivity in the Arg-177 mutants of Corynebacterium diphtheriae heme oxygenase as a consequence of in-plane heme disorder.

  2004cited by this paper
• Crystal structure of heme oxygenase-1 from cyanobacterium Synechocystis sp. PCC 6803 in complex with heme.

  2004cited by this paper
• Essential Amino Acid Residues Controlling the Unique Regioselectivity of Heme Oxygenase in Pseudomonas aeruginosa.

  2004cited by this paper
• Crystal Structure of the Dioxygen-bound Heme Oxygenase from Corynebacterium diphtheriae

  2004cited by this paper
• Bacterial Heme Oxygenases

  2004cited by this paper
• 1H NMR Investigation of the Solution Structure of Substrate-free Human Heme Oxygenase

  2004cited by this paper
• Crystal Structures of the NO- and CO-bound Heme Oxygenase from Neisseriae meningitidis

  2003cited by this paper
• Stereoselectivity of each of the three steps of the heme oxygenase reaction: hemin to meso-hydroxyhemin, meso-hydroxyhemin to verdoheme, and verdoheme to biliverdin.

  2003cited by this paper
• Crystal structures of the ferric, ferrous, and ferrous-NO forms of the Asp140Ala mutant of human heme oxygenase-1: catalytic implications.

  2003cited by this paper
• Solution 1H NMR Investigation of the Active Site Molecular and Electronic Structures of Substrate-bound, Cyanide-inhibited HmuO, a Bacterial Heme Oxygenase fromCorynebacterium diphtheriae * 210

  2003cited by this paper
• The Binding Sites on Human Heme Oxygenase-1 for Cytochrome P450 Reductase and Biliverdin Reductase*

  2003cited by this paper
• Solution 1H, 15N NMR spectroscopic characterization of substrate-bound, cyanide-inhibited human heme oxygenase: water occupation of the distal cavity.

  2003cited by this paper
• 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.

  2003cited by this paper
• Heme Oxygenase: Evolution, Structure, and Mechanism

  2002cited by this paper
• 1H NMR detection of immobilized water molecules within a strong distal hydrogen-bonding network of substrate-bound human heme oxygenase-1.

  2002cited by this paper
• Solution NMR Characterization of an Unusual Distal H-bond Network in the Active Site of the Cyanide-inhibited, Human Heme Oxygenase Complex of the Symmetric Substrate, 2,4-Dimethyldeuterohemin* 210

  2002cited by this paper
• Oxidation of heme to beta- and delta-biliverdin by Pseudomonas aeruginosa heme oxygenase as a consequence of an unusual seating of the heme.

  2002cited by this paper
• Crystal Structure of Rat Heme Oxygenase-1 in Complex with Heme Bound to Azide

  2002cited by this paper
• Homologues of Neisserial Heme Oxygenase in Gram-Negative Bacteria: Degradation of Heme by the Product of thepigA Gene of Pseudomonas aeruginosa

  2001cited by this paper
• Disruption of an Active Site Hydrogen Bond Converts Human Heme Oxygenase-1 into a Peroxidase*

  2001cited by this paper
• Crystal structure of heme oxygenase from the gram-negative pathogen Neisseria meningitidis and a comparison with mammalian heme oxygenase-1.

  2001cited by this paper
• Mechanism of heme degradation by heme oxygenase.

  2000cited by this paper
• Degradation of Heme in Gram-Negative Bacteria: the Product of the hemO Gene of Neisseriae Is a Heme Oxygenase

  2000cited by this paper
• The mechanism of heme oxygenase.

  2000cited by this paper
• Crystal structure of human heme oxygenase-1

  1999cited by this paper
• Expression and characterization of a heme oxygenase (Hmu O) from Corynebacterium diphtheriae. Iron acquisition requires oxidative cleavage of the heme macrocycle.

  1998cited by this paper
• Proton NMR investigation of substrate-bound heme oxygenase: evidence for electronic and steric contributions to stereoselective heme cleavage.

  1994cited by this paper
• Rat liver heme oxygenase. High level expression of a truncated soluble form and nature of the meso-hydroxylating species.

  1993cited by this paper
• Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions

  1992cited by this paper
• Importance of histidine residue 25 of rat heme oxygenase for its catalytic activity.

  1992cited by this paper
• Hydrogen exchange and structural dynamics of proteins and nucleic acids

  1983cited by this paper
• Real-time solvent exchange studies of the imino and amino protons of yeast phenylalanine transfer RNA by Fourier transform NMR.

  1979cited by this paper
• Features of the reaction of heme degradation catalyzed by the reconstituted microsomal heme oxygenase system.

  1978cited by this paper

• Role of propionates in substrate binding to heme oxygenase from Neisseria meningitidis: a nuclear magnetic resonance study.

  2012cites this paper
• The role of propionates in substrate binding to heme oxygenase from Neisseria meningitidis ; A NMR study

  2012cites this paper
• Influence of substrate modification and C-terminal truncation on the active site structure of substrate-bound heme oxygenase from Neisseriae meningitidis. A 1H NMR study.

  2011cites this paper
• Solution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: pertinence for determining magnetic axes in paramagnetic substrate complexes.

  2010cites this paper
• 1H NMR study of the influence of mutation on the interaction of the C-terminus with the active site in heme oxygenase from Neisseria meningitidis: implications for product release.

  2010cites this paper
• 1H NMR study of the effect of variable ligand on heme oxygenase electronic and molecular structure.

  2009cites this paper
• Mass instability in isolated recombinant FixL heme domains of Bradyrhizobium japonicum.

  2008cites this paper
• 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.

  2007cites this paper