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J. Biol. Chem., Vol. 279, Issue 16, 16535-16542, April 16, 2004

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The Crystal Structure of Synechocystis Hemoglobin with a Covalent Heme Linkage^*

Julie A. Hoy, Suman Kundu, James T. Trent, III, S. Ramaswamy, and Mark S. Hargrove¶

From the Department of Biochemistry, Biophysics, and Molecular Biology, Iowa State University, Ames, Iowa 50011 and the Department of Biochemistry, University of Iowa, Iowa City, Iowa 52242

The x-ray crystal structure of Synechocystis hemoglobin has been solved to a resolution of 1.8 Å. The conformation of this structure is surprisingly different from that of the previously reported solution structure, probably due in part to a covalent linkage between the heme 2-vinyl and His¹¹⁷ that is present in the crystal structure but not in the structure solved by NMR. Synechocystis hemoglobin is a hexacoordinate hemoglobin in which the heme iron is coordinated by both the proximal and distal histidines. It is also a member of the "truncated hemoglobin" family that is much shorter in primary structure than vertebrate and plant hemoglobins. In contrast to other truncated hemoglobins, the crystal structure of Synechocystis hemoglobin displays no "ligand tunnel" and shows that several important amino acid side chains extrude into the solvent instead of residing inside the heme pocket. The stereochemistry of hexacoordination is compared with other hexacoordinate hemoglobins and cytochromes in an effort to illuminate factors contributing to ligand affinity in hexacoordinate hemoglobins.

Received for publication, December 15, 2003 , and in revised form, January 21, 2004.

The atomic coordinates and structure factors (code 1RTX) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^* This work was supported by the National Science Foundation (Grant MCB-0077890), the U. S. Department of Agriculture (Grant 2002 35318 1217), and the Iowa State University Plant Sciences Institute. Portions of this research were carried out at the Stanford Synchrotron Radiation Laboratory, a national user facility operated by Stanford University on behalf of the U. S. Department of Energy, Office of Basic Energy Sciences. The Stanford Synchrotron Radiation Laboratory, Structural Molecular Biology Program is supported by the Department of Energy, Office of Biological and Environmental Research, and by the National Institutes of Health, National Center for Research Resources, Biomedical Technology Program, and the National Institute of General Medical Sciences. Portions of this research were carried out at the University of Iowa Protein Crystallography Facility. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^¶ To whom correspondence should be addressed. Tel.: 515-294-2616; Fax: 515-294-0453; E-mail: msh{at}iastate.edu.

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