Combined crystallographic and spectroscopic analysis of Trematomus bernacchii hemoglobin highlights analogies and differences in the peculiar oxidation pathway of antarctic fish hemoglobins

Biopolymers - Peptide Science Section

Volumn 91, Issue 12, 2009, Pages 1117-1125

  Merlino, Antonello ^a,b   Vitagliano, Luigi ^b   Howes, Barry D ^c   Verde, Cinzia ^d   Di Prisco, Guido ^d   Smulevich, Giulietta ^c   Sica, Filomena ^a,b   Vergara, Alessandro ^a,b  

^a UNIVERSITY OF NAPLES FEDERICO II   (Italy)

^b CNR   (Italy)

^c UNIVERSITY OF FLORENCE   (Italy)

^d INSTITUTE OF PROTEIN BIOCHEMISTRY   (Italy)

Author keywords

Autoxidation; Cold adaptation; Hemoglobin; Raman; X ray crystallography

Indexed keywords

AIR-EXPOSURE; BINDING STATE; COLD-ADAPTATION; ELECTRON DENSITIES; FERRIC SPECIES; GLOBAL LEVELS; HEME POCKETS; HIGH SPIN STATE; HIGH-RESOLUTION STRUCTURES; OXIDATION PATHWAY; OXIDATION PROCESS; OXIDIZED STATE; PENTACOORDINATED; RESONANCE RAMAN; SEQUENCE IDENTITY; SPECTROSCOPIC DATA; STRUCTURAL CORRELATION; STRUCTURAL SIMILARITY;

ELECTRON SPIN RESONANCE SPECTROSCOPY; HEMOGLOBIN; IRON; IRON ANALYSIS; MINERALOGY; OXIDATION; OXIDATION RESISTANCE; PORPHYRINS; SELF ASSEMBLY; SPECTROSCOPIC ANALYSIS; SPIN DYNAMICS; REACTION INTERMEDIATES;

X RAY CRYSTALLOGRAPHY;

HEMOGLOBIN; AMINO ACID; FERROUS ION; HEMOPROTEIN;

AMINO ACID SEQUENCE; ARTICLE; AUTOOXIDATION; CRYSTALLOGRAPHY; ELECTRON; FISH; NONHUMAN; PROTEIN BINDING; PROTEIN FUNCTION; PROTEIN METABOLISM; PROTEIN MODIFICATION; PROTEIN STRUCTURE; RAMAN SPECTROMETRY; SEQUENCE HOMOLOGY; STRUCTURE ANALYSIS; TREMATOMUS BERNACCHII; ANTARCTICA; CONTROLLED STUDY; CORRELATION ANALYSIS; MOLECULAR INTERACTION; PROTEIN ANALYSIS; X RAY CRYSTALLOGRAPHY;

ANIMALS; ANTARCTIC REGIONS; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; FISH PROTEINS; HEMOGLOBINS; HUMANS; HYDROGEN-ION CONCENTRATION; MODELS, MOLECULAR; OXIDATION-REDUCTION; PERCIFORMES; PROTEIN STRUCTURE, TERTIARY; SPECIES SPECIFICITY; SPECTRUM ANALYSIS; SUPEROXIDE DISMUTASE;

TREMATOMUS BERNACCHII; TREMATOMUS NEWNESI;

EID: 71749103092     PISSN: 00063525     EISSN: 10970282     Source Type: Journal    
DOI: 10.1002/bip.21206     Document Type: Article

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