Identification of two important heme site residues (cysteine 75 and histidine 77) in CooA, the CO-sensing transcription factor of Rhodospirillum rubrum.

No abstract is available for this paper.

• Publication year

  1999

• Venue

  Biochemistry

• Publication date

  1999-02-09

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1021/BI982658JPMID 10052937
• 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.

• Resonance Raman evidence for a novel charge relay activation mechanism of the CO-dependent heme protein transcription factor CooA.

  1999cited by this paper
• Heme Environmental Structure of CooA Is Modulated by the Target DNA Binding

  1998cited by this paper
• Redox-controlled Ligand Exchange of the Heme in the CO-sensing Transcriptional Activator CooA*

  1998cited by this paper
• Haem-ligand switching during catalysis in crystals of a nitrogen-cycle enzyme

  1997cited by this paper
• Characterization of ferrous FixL-nitric oxide adducts by resonance Raman spectroscopy.

  1997cited by this paper
• Interactions between substrate analogues and heme ligands in nitric oxide synthase.

  1997cited by this paper
• In vivo nickel insertion into the carbon monoxide dehydrogenase of Rhodospirillum rubrum: molecular and physiological characterization of cooCTJ

  1997cited by this paper
• CooA, a CO-sensing transcription factor from Rhodospirillum rubrum, is a CO-binding heme protein.

  1997cited by this paper
• The structure of nitric oxide synthase oxygenase domain and inhibitor complexes.

  1997cited by this paper
• Complementation analysis of mutants of nitric oxide synthase reveals that the active site requires two hemes.

  1996cited by this paper
• Characterization of the region encoding the CO-induced hydrogenase of Rhodospirillum rubrum

  1996cited by this paper
• Binding of nitric oxide and carbon monoxide to soluble guanylate cyclase as observed with Resonance raman spectroscopy.

  1996cited by this paper
• Characterization of a CO-responsive Transcriptional Activator from Rhodospirillum rubrum(*)

  1996cited by this paper
• A novel heme protein that acts as a carbon monoxide-dependent transcriptional activator in Rhodospirillum rubrum.

  1996cited by this paper
• Probing the heme iron coordination structure of alkaline chloroperoxidase.

  1996cited by this paper
• Characterization of the CO-induced, CO-tolerant hydrogenase from Rhodospirillum rubrum and the gene encoding the large subunit of the enzyme

  1996cited by this paper
• The crystal structure of chloroperoxidase: a heme peroxidase--cytochrome P450 functional hybrid.

  1995cited by this paper
• Kinase activity of oxygen sensor FixL depends on the spin state of its heme iron.

  1995cited by this paper
• Carbon monoxide-dependent growth of Rhodospirillum rubrum

  1995cited by this paper
• Carbon monoxide-induced activation of gene expression in Rhodospirillum rubrum requires the product of cooA, a member of the cyclic AMP receptor protein family of transcriptional regulators

  1995cited by this paper
• The Oxygen Sensor Protein, FixL, of Rhizobium meliloti

  1995cited by this paper
• Nitric oxide: a physiologic messenger molecule.

  1994cited by this paper
• Carbon monoxide: a putative neural messenger.

  1993cited by this paper
• Roles of proximal ligand in heme proteins: replacement of proximal histidine of human myoglobin with cysteine and tyrosine by site-directed mutagenesis as models for P-450, chloroperoxidase, and catalase.

  1993cited by this paper
• Resonance Raman investigations of Escherichia coli-expressed Pseudomonas putida cytochrome P450 and P420.

  1992cited by this paper
• Genetic and physiological characterization of the Rhodospirillum rubrum carbon monoxide dehydrogenase system

  1992cited by this paper
• Does carbon monoxide have a physiological function?

  1991cited by this paper
• Activation of the nickel-deficient carbon monoxide dehydrogenase from Rhodospirillum rubrum: kinetic characterization and reductant requirement.

  1990cited by this paper
• Overproduction and dissection of proteins by the expression-cassette polymerase chain reaction.

  1990cited by this paper
• Regulation of carbon monoxide dehydrogenase and hydrogenase in Rhodospirillum rubrum: effects of CO and oxygen on synthesis and activity

  1989cited by this paper
• Protein determination using bicinchoninic acid in the presence of sulfhydryl reagents.

  1988cited by this paper
• Site-directed mutageneses of rat liver cytochrome P-450d: axial ligand and heme incorporation.

  1988cited by this paper
• Purification and characterization of carbon monoxide dehydrogenase, a nickel, zinc, iron-sulfur protein, from Rhodospirillum rubrum.

  1987cited by this paper
• Measurement of protein using bicinchoninic acid.

  1985cited by this paper
• Hemoprotein H-450 identified as a form of cytochrome P-450 having an endogenous ligand at the 6th coordination position of the heme.

  1984cited by this paper
• Structural studies of hemoglobin Saint Etienne beta 92 (F8) his --> GLN: A new abnormal hemoglobin with loss of beta proximal histidine and absence of heme on the beta chains.

  1972cited by this paper
• A spectrophotometric method for the simultaneous determination of myoglobin and hemoglobin in extracts of human muscle.

  1948cited by this paper

• Spectroscopic Interrogation of Thiolate Hydrogen Bonding in the CO Sensor Protein CooA: Implications for Thiolate Ligation Stability and Cytochrome P450 Function

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  2025cites this paper
• New insights into the signal transduction mechanism of O2-sensing FixL and other biological heme-based sensor proteins.

  2024cites this paper
• Probing conformational dynamics of DNA binding by CO-sensing transcription factor, CooA.

  2024cites this paper
• Carbon Monoxide-Sensing Transcription Factors: Regulators of Microbial Carbon Monoxide Oxidation Pathway Gene Expression

  2023cites this paper
• Characterization of Heme Binding to PEFR, A Marr Transcriptional Regulator

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  2022cites this paper
• Quaternary Structure and Deoxyribonucleic Acid-Binding Properties of the Heme-Dependent, CO-Sensing Transcriptional Regulator PxRcoM.

  2022cites this paper
• Reaction of Thiosulfate Dehydrogenase with a Substrate Mimic Induces Dissociation of the Cysteine Heme Ligand Giving Insights into the Mechanism of Oxidative Catalysis

  2022cites this paper
• Electron Paramagnetic Resonance Spectroscopy as a Probe of Hydrogen Bonding in Heme-Thiolate Proteins.

  2019cites this paper
• Redox-Based Transcriptional Regulation in Prokaryotes: Revisiting Model Mechanisms

  2019cites this paper
• Spectroscopic evidence supporting neutral thiol ligation to ferrous heme iron

  2018cites this paper
• Do nitric oxide, carbon monoxide and hydrogen sulfide really qualify as ‘gasotransmitters’ in bacteria?

  2018cites this paper
• Site‐directed spin label electron paramagnetic resonance spectroscopy as a probe of conformational dynamics in the Fe(III) “locked‐off” state of the CO‐sensing transcription factor CooA

  2018cites this paper
• What Can Be Learned from Nuclear Resonance Vibrational Spectroscopy: Vibrational Dynamics and Hemes

  2017cites this paper
• CO and NO bind to Fe(II) DiGeorge critical region 8 heme but do not restore primary microRNA processing activity

  2016cites this paper
• Met104 is the CO-replaceable ligand at Fe(II) heme in the CO-sensing transcription factor BxRcoM-1

  2016cites this paper
• A Study of the Dynamics of the Heme Pocket and C-helix in CooA upon CO Dissociation Using Time-Resolved Visible and UV Resonance Raman Spectroscopy.

  2016cites this paper
• Functional divergence of heme-thiolate proteins: a classification based on spectroscopic attributes.

  2015cites this paper
• Gaseous O2, NO, and CO in signal transduction: structure and function relationships of heme-based gas sensors and heme-redox sensors.

  2015cites this paper
• Redox-dependent stability, protonation, and reactivity of cysteine-bound heme proteins

  2014cites this paper
• Improvement of carbon monoxide-dependent hydrogen production activity in Citrobacter amalonaticus Y19 by over-expressing the CO-sensing transcriptional activator, CooA

  2014cites this paper
• The Diagnostic Vibrational Signature of Pentacoordination in Heme Carbonyls

  2014cites this paper
• Haem-based sensors: a still growing old superfamily.

  2013cites this paper
• A Heme-based Redox Sensor in the Methanogenic Archaeon Methanosarcina acetivorans*

  2013cites this paper
• Recent History of Heme-Containing Proteins: Advances in Structure, Functions, and Reaction Intermediate Determination

  2013cites this paper
• Identification of proximal and distal axial ligands in Leishmania major pseudoperoxidase.

  2013cites this paper
• A selective fluorescent probe for carbon monoxide imaging in living cells.

  2012cites this paper
• Identification of Cys94 as the distal ligand to the Fe(III) heme in the transcriptional regulator RcoM-2 from Burkholderia xenovorans

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  2009cites this paper
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  2009influential citation
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  2008cites this paper
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  2008cites this paper
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  2007cites this paper
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  2007cites this paper
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  2006cites this paper
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  2006cites this paper
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  2006cites this paper
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  2006cites this paper
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  2006cites this paper
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  2006cites this paper
• Heme Displacement Mechanism of CooA Activation

  2006cites this paper
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  2005cites this paper
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  2005cites this paper
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  2005cites this paper
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  2004cites this paper
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  2004cites this paper
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  2004cites this paper
• Changing the Ligand Specificity of CooA, a Highly Specific Heme-based CO Sensor*

  2004cites this paper
• Dynamics of Carbon Monoxide Binding to CooA*

  2004cites this paper
• Roles of Heme Axial Ligands in the Regulation of CO Binding to CooA*

  2004cites this paper
• Investigation of the role of the N-terminal proline, the distal heme ligand in the CO sensor CooA.

  2004cites this paper
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  2003cites this paper
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  2003cites this paper
• The Role of the Hydrophobic Distal Heme Pocket of CooA in Ligand Sensing and Response*

  2003cites this paper
• [Molecular biology of iron in nutritional science].

  2003cites this paper
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  2003cites this paper
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  2001cites this paper
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  2001cites this paper
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  2001cites this paper
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  2001cites this paper
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  2001cites this paper
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  2001cites this paper
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  2001cites this paper
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  2001cites this paper
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  2001cites this paper
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  2001cites this paper
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  2001cites this paper
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  2000cites this paper
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  2000cites this paper
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