Abstract

The two available crystallographic structures of cobalamin dependent enzymes, the 27 kDa fragment of the methylcobalamin-dependent enzyme, methionine synthase, from Escherichia coli [C. L. Drennan et al. Science, 266, 1669 (1994)] and the 5?-deoxyadenosylcobalamin-dependent enzyme methylmalonyl-coenzyme A mutase from Propionibacterium shermanii [F. Mancia et al. Structure, 4, 339 (1996)], show striking similarities despite the differences in reaction mechanism. In particular, the 5,6-dimethylbenzimidazole group is detached and replaced by a histidine group of the enzyme. We have analyzed Extended X-ray Absorption Fine Structure (EXAFS) spectroscopic data for both 5?-deoxyadenosylcobalamin and aquocobalamin bound to methylmalonyl-coenzyme A mutase in the absence of substrate. The analysis is conducted with a suite of programs called AUTOFIT 1.0 [Chance et al., Biochemistry, 1996, 35, 9014], which allows an evenhanded comparison of the goodness-of-fit of the EXAFS data to a varied grid of simulations based on the ab initio EXAFS code FEFF 6.01. The x-ray edge data indicate an increase in effective nuclear charge of the metal ion of the enzyme bound 5?-deoxyadeonsylcobalamin compared to the corresponding free cobalamin and the EXAFS results show small decreases in equatorial and no significant change in the Co-C bond length.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR001633-17
Application #
6205769
Study Section
Project Start
1999-09-01
Project End
2000-08-31
Budget Start
1998-10-01
Budget End
1999-09-30
Support Year
17
Fiscal Year
1999
Total Cost
Indirect Cost

  Institution

Name
Albert Einstein College of Medicine
Department
Type
DUNS #
009095365
City
Bronx
State
NY
Country
United States
Zip Code
10461

  Publications

Vongsvivut, Jitraporn; Fernandez, Jason; Ekgasit, Sanong et al. (2004) Characterization of supported cylinder-planar germanium waveguide sensors with synchrotron infrared radiation. Appl Spectrosc 58:143-51
Masip, Lluis; Pan, Jonathan L; Haldar, Suranjana et al. (2004) An engineered pathway for the formation of protein disulfide bonds. Science 303:1185-9
Huang, Raymond Y; Miller, Lisa M; Carlson, Cathy S et al. (2003) In situ chemistry of osteoporosis revealed by synchrotron infrared microspectroscopy. Bone 33:514-21
Rashidzadeh, Hassan; Khrapunov, Sergei; Chance, Mark R et al. (2003) Solution structure and interdomain interactions of the Saccharomyces cerevisiae ""TATA binding protein"" (TBP) probed by radiolytic protein footprinting. Biochemistry 42:3655-65
Uchida, Takeshi; Takamoto, Keiji; He, Qin et al. (2003) Multiple monovalent ion-dependent pathways for the folding of the L-21 Tetrahymena thermophila ribozyme. J Mol Biol 328:463-78
Taylor, Colleen M; Watton, Stephen P; Bryngelson, Peter A et al. (2003) Inner-sphere complexation of cobalt(II) 2,9-dimethyl-1,10-phenanthroline ([Co(neo)]2+) with commercial and sol-gel derived silica gel surfaces. Inorg Chem 42:312-20
Chance, Mark R; Bresnick, Anne R; Burley, Stephen K et al. (2002) Structural genomics: a pipeline for providing structures for the biologist. Protein Sci 11:723-38
Maleknia, Simin D; Kiselar, Janna G; Downard, Kevin M (2002) Hydroxyl radical probe of the surface of lysozyme by synchrotron radiolysis and mass spectrometry. Rapid Commun Mass Spectrom 16:53-61
Marinkovic, N S; Huang, R; Bromberg, P et al. (2002) Center for Synchrotron Biosciences' U2B beamline: an international resource for biological infrared spectroscopy. J Synchrotron Radiat 9:189-97
Huang, R Y; Miller, L M; Carlson, C S et al. (2002) Characterization of bone mineral composition in the proximal tibia of cynomolgus monkeys: effect of ovariectomy and nandrolone decanoate treatment. Bone 30:492-7

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