Hemoglobins of the Lucina pectinata /bacteria symbiosis. 2. An electron paramagnetic resonance and optical spectral study of the ferric proteins

Hemoglobins of the Lucina pectinata /bacteria symbiosis. 2. An electron paramagnetic resonance and optical spectral study of the ferric proteins

We report an optical and EPR spectral study of three hemoglobins, Hb I, II, and III, from the gill of the clam Lucina pectinata . Hemoglobin I reacts much more avidly with hydrogen sulfide than do Hbs II and III. The proximal ligand to the heme iron of each hemoglobin is histidyl imidazole.

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Veröffentlicht in:The Journal of biological chemistry 1990-09, Vol.265 (27), p.16054-16059
Hauptverfasser: Kraus, D W, Wittenberg, J B, Lu, Jing-Fen, Peisach, J
Format: Artikel
Sprache:eng
Schlagworte:
chemical reactions
E.S.R
haemoglobins
hemoglobin
ligands
Lucina pectinata
Marine
marine molluscs
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Zusammenfassung:We report an optical and EPR spectral study of three hemoglobins, Hb I, II, and III, from the gill of the clam Lucina pectinata . Hemoglobin I reacts much more avidly with hydrogen sulfide than do Hbs II and III. The proximal ligand to the heme iron of each hemoglobin is histidyl imidazole.
ISSN:0021-9258