The Crystal Structure of Peroxymyoglobin Generated Through Cryoradiolytic Reduction of Myoglobin Compound III During Data Collection.
作者： Hans-Petter Hersleth , Ya-Wen Hsiao , Ulf Ryde , Carl Henrik Görbitz , K. Kristoffer Andersson
DOI: 10.1042/BJ20070921
关键词: Oxygen binding 、 Leaving group 、 Oxygen transport 、 Crystallography 、 Peroxide 、 Hydrogen peroxide 、 Chemistry 、 Crystal structure 、 Myoglobin 、 Molecule
摘要: Myoglobin has the ability to react with hydrogen peroxide, generating high-valent complexes similar peroxidases (compounds I and II), in presence of excess peroxide a third intermediate, compound III, an oxymyoglobin-type structure is generated from II. The III is, however, easily one-electron reduced peroxymyoglobin by synchrotron radiation during crystallograpic data collection. We have solved 1.30 angstrom (1 angstrom= 0.1 nin) resolution crystal which isoelectric 0 Fe-O distance 1.8 O-O bond 1.3 accordance Fe-II-O-O- (or Fe-III-O-O2-) structure. generation peroxy intermediate through reduction X-rays shows importance using single-crystal microspectrophotometry when doing crystallography on metal loproteins. After having collected crystallographic peroxy-generated myoglobin crystal, we were able (by short annealing) break leading formation These results indicate that cryoradiolytic-generated biologically relevant its conversion into II upon heating. Additionally, observed Xe1 site occupied water molecule, might be leaving group reaction. (Less)
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Friedrich Schotte, Manho Lim, Timothy A Jackson, Aleksandr V Smirnov, Jayashree Soman, John S Olson, George N Phillips Jr, Michael Wulff, Philip A Anfinrud, Watching a Protein as it Functions with 150-ps Time-Resolved X-ray Crystallography Science. ,vol. 300, pp. 1944- 1947 ,(2003) , 10.1126/SCIENCE.1078797
Adrian J. Mulholland, The QM/MM Approach to Enzymatic Reactions Theoretical and Computational Chemistry. ,vol. 9, pp. 597- 653 ,(2001) , 10.1016/S1380-7323(01)80015-7
Zbyszek Otwinowski, Wladek Minor, Processing of X-ray diffraction data collected in oscillation mode Methods in Enzymology. ,vol. 276, pp. 307- 326 ,(1997) , 10.1016/S0076-6879(97)76066-X
T.L. Poulos, J. Kraut, The stereochemistry of peroxidase catalysis. Journal of Biological Chemistry. ,vol. 255, pp. 8199- 8205 ,(1980) , 10.1016/S0021-9258(19)70630-9
Robert F. Tilton, Irwin D. Kuntz, Gregory A. Petsko, Cavities in proteins: structure of a metmyoglobin-xenon complex solved to 1.9 A. Biochemistry. ,vol. 23, pp. 2849- 2857 ,(1984) , 10.1021/BI00308A002
H. Frauenfelder, B. H. McMahon, R. H. Austin, K. Chu, J. T. Groves, The role of structure, energy landscape, dynamics, and allostery in the enzymatic function of myoglobin Proceedings of the National Academy of Sciences of the United States of America. ,vol. 98, pp. 2370- 2374 ,(2001) , 10.1073/PNAS.041614298
J.O. Alben, F.G. Fiamingo, A.A. Croteau, C.F. Hemann, K.A. Powell, V.M. Molleran, S. Park, X-ray absorption spectroscopy of myoglobin and iron prophyrin derivatives Physica B: Condensed Matter. ,vol. 158, pp. 87- 89 ,(1989) , 10.1016/0921-4526(89)90208-1
Kristina Nilsson, David Lecerof, Emma Sigfridsson, Ulf Ryde, None, An automatic method to generate force-field parameters for hetero-compounds. Acta Crystallographica Section D-biological Crystallography. ,vol. 59, pp. 274- 289 ,(2003) , 10.1107/S0907444902021431
Garib N. Murshudov, Albina I. Grebenko, James A. Brannigan, Alfred A. Antson, Vladimir V. Barynin, Guy G. Dodson, Zbigniew Dauter, Keith S. Wilson, William R. Melik-Adamyan, The Structures of Micrococcus Lysodeikticus Catalase, its Ferryl Intermediate (Compound II) and Nadph Complex. Acta Crystallographica Section D-biological Crystallography. ,vol. 58, pp. 1972- 1982 ,(2002) , 10.1107/S0907444902016566
Ilia G. Denisov, Thomas M. Makris, Stephen G. Sligar, Formation and decay of hydroperoxo-ferric heme complex in horseradish peroxidase studied by cryoradiolysis Journal of Biological Chemistry. ,vol. 277, pp. 42706- 42710 ,(2002) , 10.1074/JBC.M207949200