Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Science 24 January 1997:
Vol. 275. no. 5299, pp. 515 - 518
DOI: 10.1126/science.275.5299.515
Prev | Table of Contents | Next

Reports

An Fe2IVO2 Diamond Core Structure for the Key Intermediate Q of Methane Monooxygenase

Lijin Shu, Jeremy C. Nesheim, Karl Kauffmann, Eckard Münck, John D. Lipscomb, Lawrence Que Jr. *

A new paradigm for oxygen activation is required for enzymes such as methane monooxygenase (MMO), for which catalysis depends on a nonheme diiron center instead of the more familiar Fe-porphyrin cofactor. On the basis of precedents from synthetic diiron complexes, a high-valent Fe2(µ-O)2 diamond core has been proposed as the key oxidizing species for MMO and other nonheme diiron enzymes such as ribonucleotide reductase and fatty acid desaturase. The presence of a single short Fe-O bond (1.77 angstroms) per Fe atom and an Fe-Fe distance of 2.46 angstroms in MMO reaction intermediate Q, obtained from extended x-ray absorption fine structure and Mössbauer analysis, provides spectroscopic evidence that the diiron center in Q has an Fe2IVO2 diamond core.

L. Shu and L. Que Jr., Department of Chemistry and Center for Metals in Biocatalysis, University of Minnesota, Minneapolis, MN 55455, USA.
J. C. Nesheim and J. D. Lipscomb, Department of Biochemistry, Medical School, and Center for Metals in Biocatalysis, University of Minnesota, Minneapolis, MN 55455, USA.
K. Kauffmann and E. Münck, Department of Chemistry, Carnegie Mellon University, Pittsburgh, PA 15213, USA.
*   To whom correspondence should be addressed. E-mail: QUE{at}chem.umn.edu

Read the Full Text


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Kinetic characterization of the soluble butane monooxygenase from Thauera butanivorans, formerly 'Pseudomonas butanovora'.
R. B. Cooley, B. L. Dubbels, L. A. Sayavedra-Soto, P. J. Bottomley, and D. J. Arp (2009)
Microbiology 155, 2086-2096
   Abstract »    Full Text »    PDF »
Redox Intermediates of the Mn-Fe Site in Subunit R2 of Chlamydia trachomatis Ribonucleotide Reductase: AN X-RAY ABSORPTION AND EPR STUDY.
N. Voevodskaya, F. Lendzian, O. Sanganas, A. Grundmeier, A. Graslund, and M. Haumann (2009)
J. Biol. Chem. 284, 4555-4566
   Abstract »    Full Text »    PDF »
Insights into the P-to-Q conversion in the catalytic cycle of methane monooxygenase from a synthetic model system.
G. Xue, A. T. Fiedler, M. Martinho, E. Munck, and L. Que Jr (2008)
PNAS 105, 20615-20620
   Abstract »    Full Text »    PDF »
The ferritin Fe2 site at the diiron catalytic center controls the reaction with O2 in the rapid mineralization pathway.
T. Tosha, M. R. Hasan, and E. C. Theil (2008)
PNAS 105, 18182-18187
   Abstract »    Full Text »    PDF »
A catalytic di-heme bis-Fe(IV) intermediate, alternative to an Fe(IV)=O porphyrin radical.
X. Li, R. Fu, S. Lee, C. Krebs, V. L. Davidson, and A. Liu (2008)
PNAS 105, 8597-8600
   Abstract »    Full Text »    PDF »
Synthetic iron-oxo "diamond core" mimics structure of key intermediate in methane monooxygenase catalytic cycle.
T. C. Brunold (2007)
PNAS 104, 20641-20642
   Full Text »    PDF »
A synthetic precedent for the [FeIV2({micro}-O)2] diamond core proposed for methane monooxygenase intermediate Q.
G. Xue, D. Wang, R. De Hont, A. T. Fiedler, X. Shan, E. Munck, and L. Que Jr. (2007)
PNAS 104, 20713-20718
   Abstract »    Full Text »    PDF »
Mutagenesis of the "Leucine Gate" To Explore the Basis of Catalytic Versatility in Soluble Methane Monooxygenase.
E. Borodina, T. Nichol, M. G. Dumont, T. J. Smith, and J. C. Murrell (2007)
Appl. Envir. Microbiol. 73, 6460-6467
   Abstract »    Full Text »    PDF »
Hydroxylation of C-H bonds at carboxylate-bridged diiron centres.
S. J Lippard (2005)
Phil Trans R Soc A 363, 861-877
   Abstract »    Full Text »    PDF »
Bioinorganic Chemistry Special Feature: Opening protein pores with chaotropes enhances Fe reduction and chelation of Fe from the ferritin biomineral.
X. Liu, W. Jin, and E. C. Theil (2003)
PNAS 100, 3653-3658
   Abstract »    Full Text »    PDF »
Bioinorganic Chemistry Special Feature: An FeIV==O complex of a tetradentate tripodal nonheme ligand.
M. H. Lim, J.-U. Rohde, A. Stubna, M. R. Bukowski, M. Costas, R. Y. N. Ho, E. Munck, W. Nam, and L. Que Jr. (2003)
PNAS 100, 3665-3670
   Abstract »    Full Text »    PDF »
Hydrogen Peroxide-coupled cis-Diol Formation Catalyzed by Naphthalene 1,2-Dioxygenase.
M. D. Wolfe and J. D. Lipscomb (2003)
J. Biol. Chem. 278, 829-835
   Abstract »    Full Text »    PDF »
Iron uptake in ferritin is blocked by binding of [Cr(TREN)(H2O)(OH)]2+, a slow dissociating model for [Fe(H2O)6]2+.
C. M. Barnes, E. C. Theil, and K. N. Raymond (2002)
PNAS 99, 5195-5200
   Abstract »    Full Text »    PDF »
A Short Fe-Fe Distance in Peroxodiferric Ferritin: Control of Fe Substrate Versus Cofactor Decay?.
J. Hwang, C. Krebs, B. H. Huynh, D. E. Edmondson, E. C. Theil, and J. E. Penner-Hahn (2000)
Science 287, 122-125
   Abstract »    Full Text »
Oxidation of Ultrafast Radical Clock Substrate Probes by the Soluble Methane Monooxygenase from Methylococcus capsulatus (Bath).
A. M. Valentine, M.-H. LeTadic-Biadatti, P. H. Toy, M. Newcomb, and S. J. Lippard (1999)
J. Biol. Chem. 274, 10771-10776
   Abstract »    Full Text »    PDF »
Kinetic Evidence That a Radical Transfer Pathway in Protein R2 of Mouse Ribonucleotide Reductase Is Involved in Generation of the Tyrosyl Free Radical.
P. P. Schmidt, U. Rova, B. Katterle, L. Thelander, and A. Graslund (1998)
J. Biol. Chem. 273, 21463-21472
   Abstract »    Full Text »    PDF »
Identification of Non-Heme Diiron Proteins That Catalyze Triple Bond and Epoxy Group Formation.
M. Lee, M. Lenman, A. Bana, M. Bafor, S. Singh, M. Schweizer, R. Nilsson, C. Liljenberg, A. Dahlqvist, P. Gummeson, et al. (1998)
Science 280, 915-918
   Abstract »    Full Text »
Oxidation of Methyl-Substituted Naphthalenes: Pathways in a Versatile Sphingomonas paucimobilis Strain.
T. K. Dutta, S. A. Selifonov, and I. C. Gunsalus (1998)
Appl. Envir. Microbiol. 64, 1884-1889
   Abstract »    Full Text »    PDF »
Single Turnover Chemistry and Regulation of O2 Activation by the Oxygenase Component of Naphthalene 1,2-Dioxygenase.
M. D. Wolfe, J. V. Parales, D. T. Gibson, and J. D. Lipscomb (2001)
J. Biol. Chem. 276, 1945-1953
   Abstract »    Full Text »    PDF »
Oxygen Kinetic Isotope Effects in Soluble Methane Monooxygenase.
S. S. Stahl, W. A. Francisco, M. Merkx, J. P. Klinman, and S. J. Lippard (2001)
J. Biol. Chem. 276, 4549-4553
   Abstract »    Full Text »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)