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J Biol Chem, Vol. 274, Issue 11, 6898-6910, March 12, 1999

Chlamydomonas Chloroplast Ferrous Hemoglobin
HEME POCKET STRUCTURE AND REACTIONS WITH LIGANDS

Manon Couture, Tapan Kanti Das^§, H. Caroline Lee^§, Jack Peisach^§, Denis L. Rousseau^§, Beatrice A. Wittenberg^§, Jonathan B. Wittenberg^§, and Michel Guertin

From the  Department of Biochemistry, Faculty of Sciences and Engineering, Laval University, Quebec G1K 7P4, Canada and the ^§ Department of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, New York 10461

We report the optical and resonance Raman spectral characterization of ferrous recombinant Chlamydomonas LI637 hemoglobin. We show that it is present in three pH-dependent equilibrium forms including a 4-coordinate species at acid pH, a 5-coordinate high spin species at neutral pH, and a 6-coordinate low spin species at alkaline pH. The proximal ligand to the heme is the imidazole group of a histidine. Kinetics of the reactions with ligands were determined by stopped-flow spectroscopy. At alkaline pH, combination with oxygen, nitric oxide, and carbon monoxide displays a kinetic behavior that is interpreted as being rate-limited by conversion of the 6-coordinate form to a reactive 5-coordinate form. At neutral pH, combination rates of the 5-coordinate form with oxygen and carbon monoxide were much faster (>10⁷ µM¹ s¹). The dissociation rate constant measured for oxygen is among the slowest known, 0.014 s¹, and is independent of pH. Replacement of the tyrosine 63 (B10) by leucine or of the putative distal glutamine by glycine increases the dissociation rate constant 70- and 30-fold and increases the rate of autoxidation 20- and 90-fold, respectively. These results are consistent with at least two hydrogen bonds stabilizing the bound oxygen molecule, one from tyrosine B10 and the other from the distal glutamine. In addition, the high frequency (232 cm¹) of the iron-histidine bond suggests a structure that lacks any proximal strain thus contributing to high ligand affinity.

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