Structural determinants of ligand binding in truncated hemoglobins: Resonance Raman spectroscopy of the native states and their carbon monoxide and hydroxide complexes

No abstract is available for this paper.

• Publication year

  2018

• Venue

  Biopolymers

• Publication date

  2018-03-30

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1002/bip.23114PMID 29603146
• 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.

• Coexistence of multiple globin genes conferring protection against nitrosative stress to the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125.

  2018cited by this paper
• Access and Binding of H2S to Hemeproteins: The Case of HbI of Lucina pectinata.

  2016cited by this paper
• Evolutionary and Functional Relationships in the Truncated Hemoglobin Family

  2016cited by this paper
• The N‐terminal pre‐A region of Mycobacterium tuberculosis 2/2HbN promotes NO‐dioxygenase activity

  2016cited by this paper
• Bridging Theory and Experiment to Address Structural Properties of Truncated Haemoglobins: Insights from Thermobifida fusca HbO.

  2015cited by this paper
• Structural flexibility of the heme cavity in the cold‐adapted truncated hemoglobin from the Antarctic marine bacterium Pseudoalteromonas haloplanktis TAC125

  2015cited by this paper
• Interplay of the H-bond donor-acceptor role of the distal residues in hydroxyl ligand stabilization of Thermobifida fusca truncated hemoglobin.

  2014cited by this paper
• Nitrosylation Mechanisms of Mycobacterium tuberculosis and Campylobacter jejuni Truncated Hemoglobins N, O, and P

  2014cited by this paper
• Small ligand-globin interactions: reviewing lessons derived from computer simulation.

  2013cited by this paper
• Bacterial and archaeal globins - a revised perspective.

  2013cited by this paper
• Distinct structural and redox properties of the heme active site in bacterial dye decolorizing peroxidase-type peroxidases from two subfamilies: resonance Raman and electrochemical study.

  2013cited by this paper
• The diversity of 2/2 (truncated) globins.

  2013cited by this paper
• The globins of cyanobacteria and algae.

  2013cited by this paper
• H-bonding networks of the distal residues and water molecules in the active site of Thermobifida fusca hemoglobin.

  2013cited by this paper
• Antarctic bacterial haemoglobin and its role in the protection against nitrogen reactive species.

  2013cited by this paper
• Ligand-rebinding kinetics of 2/2 hemoglobin from the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125.

  2013cited by this paper
• The peculiar heme pocket of the 2/2 hemoglobin of cold-adapted Pseudoalteromonas haloplanktis TAC125

  2011cited by this paper
• Ligand‐ and proton‐linked conformational changes of the ferrous 2/2 hemoglobin of Pseudoalteromonas haloplanktis TAC125

  2011cited by this paper
• Structural characterization of a group II 2/2 hemoglobin from the plant pathogen Agrobacterium tumefaciens.

  2011cited by this paper
• Occurrence and formation of endogenous histidine hexa‐coordination in cold‐adapted hemoglobins

  2011cited by this paper
• Differences in coordination states of substituted tyrosine residues and quaternary structures among hemoglobin M probed by resonance Raman spectroscopy

  2010cited by this paper
• Structure and reactivity of hexacoordinate hemoglobins.

  2010cited by this paper
• Heme pocket structural properties of a bacterial truncated hemoglobin from Thermobifida fusca.

  2010cited by this paper
• Catalytic peroxidation of nitrogen monoxide and peroxynitrite by globins

  2009cited by this paper
• The bis-histidyl complex in hemoproteins: A detailed conformational analysis of database protein structures and the case of Antarctic fish hemoglobins.

  2009cited by this paper
• Structural characterization of the hemophore HasAp from Pseudomonas aeruginosa: NMR spectroscopy reveals protein-protein interactions between Holo-HasAp and hemoglobin.

  2009cited by this paper
• Peroxynitrite detoxification by ferryl Mycobacterium leprae truncated hemoglobin O.

  2009cited by this paper
• Deciphering the Structural Role of Histidine 83 for Heme Binding in Hemophore HasA*

  2008cited by this paper
• Hemoglobins from Mycobacterium tuberculosis and Campylobacter jejuni: a comparative study with resonance Raman spectroscopy.

  2008cited by this paper
• The truncated hemoglobins in the Antarctic psychrophilic bacterium Pseudoalteromonas haloplanktis TAC125.

  2007cited by this paper
• A novel thermostable hemoglobin from the actinobacterium Thermobifida fusca

  2005cited by this paper
• CO as a vibrational probe of heme protein active sites.

  2005cited by this paper
• Complexes of horseradish peroxidase with formate, acetate, and carbon monoxide.

  2005cited by this paper
• Structural and functional properties of hemoglobins from unicellular organisms as revealed by resonance Raman spectroscopy.

  2005cited by this paper
• Characterization of the periplasmic heme-binding protein shut from the heme uptake system of Shigella dysenteriae.

  2005cited by this paper
• Nitric oxide dioxygenase function and mechanism of flavohemoglobin, hemoglobin, myoglobin and their associated reductases.

  2005cited by this paper
• Structural bases for heme binding and diatomic ligand recognition in truncated hemoglobins.

  2005cited by this paper
• Truncated Hemoglobins: A New Family of Hemoglobins Widely Distributed in Bacteria, Unicellular Eukaryotes, and Plants* 210

  2002cited by this paper
• Unique ligand-protein interactions in a new truncated hemoglobin from Mycobacterium tuberculosis.

  2002cited by this paper
• Structural investigations of the hemoglobin of the cyanobacterium Synechocystis PCC6803 reveal a unique distal heme pocket.

  2000cited by this paper
• Hydroxide Rather Than Histidine Is Coordinated to the Heme in Five-coordinate Ferric Scapharca inaequivalvisHemoglobin*

  1999cited by this paper
• BOUND CO IS A MOLECULAR PROBE OF ELECTROSTATIC POTENTIAL IN THE DISTAL POCKET OF MYOGLOBIN

  1999cited by this paper
• Formation of a Five-Coordinate Hydroxide-Bound Heme in the His93Gly Mutant of Sperm Whale Myoglobin.

  1999cited by this paper
• The Heme Environment in Barley Hemoglobin*

  1999cited by this paper
• Identification of the ligands to the ferric heme of Chlamydomonas chloroplast hemoglobin: evidence for ligation of tyrosine-63 (B10) to the heme.

  1999cited by this paper
• The structure of carbonyl horseradish peroxidase: spectroscopic and kinetic characterization of the carbon monoxide complexes of His-42 → Leu and Arg-38 → Leu mutants

  1998cited by this paper
• The distal cavity structure of carbonyl horseradish peroxidase as probed by the resonance Raman spectra of His 42 Leu and Arg 38 Leu mutants.

  1998cited by this paper
• Spin-state equilibria and axial ligand bonding in FixL hydroxide: a resonance raman study

  1998cited by this paper
• Mutation of distal residues of horseradish peroxidase: influence on substrate binding and cavity properties.

  1997cited by this paper
• Spectroscopic evidence for a conformational transition in horseradish peroxidase at very low pH.

  1997cited by this paper
• Spin state and axial ligand bonding in the hydroxide complexes of metmyoglobin, methemoglobin, and horseradish peroxidase at room and low temperatures.

  1994cited by this paper
• How far can proteins bend the FeCO unit? Distal polar and steric effects in heme proteins and models

  1994cited by this paper
• Conformational change and histidine control of heme chemistry in cytochrome c peroxidase: resonance Raman evidence from Leu-52 and Gly-181 mutants of cytochrome c peroxidase.

  1991cited by this paper
• Characteristics in tyrosine coordinations of four hemoglobins M probed by resonance Raman spectroscopy.

  1989cited by this paper
• Cytochrome c peroxidase mutant active site structures probed by resonance Raman and infrared signatures of the CO adducts.

  1988cited by this paper
• Is bound carbonyl linear or bent in heme proteins? Evidence from resonance Raman and infrared spectroscopic data.

  1988cited by this paper
• Two types of conformers with distinct Fe-C-O configuration in the ferrous CO complex of horseradish peroxidase. Resonance Raman and infarared spectroscopic studies with native and deuteroheme-substituted enzymes.

  1987cited by this paper
• Alternative carbon monoxide binding modes for horseradish peroxidase studied by resonance Raman spectroscopy.

  1986cited by this paper
• Two CO binding modes for HRPCO and CCPCO: Raman evidence of CO pressure and pH dependence

  1986cited by this paper
• Infrared spectroscopic evidence of hydrogen bonding between carbon monoxide and protein in carbonylhorseradish peroxidase C

  1983cited by this paper
• Leghemoglobin. An electron paramagnetic resonance and optical spectral study of the free protein and its complexes with nicotinate and acetate.

  1976cited by this paper
• Infrared spectroscopic studies of carbonyl horseradish peroxidases.

  1976cited by this paper

• A functional and applied perspective of Vitreoscilla hemoglobin: from oxygen carriage to biotechnological innovation

  2025cites this paper
• Kinetic and dynamical properties of truncated hemoglobins of the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125

  2024cites this paper
• The effect of pH and nitrite on the haem pocket of GLB-33, a globin-coupled neuronal transmembrane receptor of Caenorhabditis elegans.

  2023cites this paper
• Lucina pectinata oxyhemoglobin (II-III) heterodimer pH susceptibility.

  2020cites this paper
• Conformational Flexibility Drives Cold Adaptation in Pseudoalteromonas haloplanktis TAC125 Globins

  2020influential citation
• Solution and crystal phase resonance Raman spectroscopy: Valuable tools to unveil the structure and function of heme proteins

  2019cites this paper
• Resonance Raman optical activity of the imidazole–Myoglobin complex: Titrating enhancement

  2019cites this paper