How coenzyme B12 radicals are generated: the crystal structure of methylmalonyl-coenzyme A mutase at 2 å resolution

Lenhert, 1961, Structure of the 5,6-dimethylbenzimidazolylcobamide coenzyme, Nature, 192, 937, 10.1038/192937a0

Halpern, 1985, Mechanisms of coenzyme B12-dependent rearrangements, Science, 227, 869, 10.1126/science.2857503

Pratt, 1993, Nature's design and use of catalysis based on Co and the macrocyclic corrin ligand: 4×109 years of coordination chemistry, Pure & Appl. Chem, 65, 1513, 10.1351/pac199365071513

Rétey, 1966, Coenzym B12 als gemeinsamer wasserstoffüberträger der dioldehydrase und der methylmalonyl-CoA mutase reaktion, Experientia, 22, 783, 10.1007/BF01897408

Cardinale, 1967, Mechanistic similarities in the reactions catalysed by diol dehydrase and methylmalonyl-CoA mutase, Biochim. Biophys. Acta, 132, 517, 10.1016/0005-2744(67)90173-8

Cockle, 1972, The detection of intermediates during the conversion of propane-1,2-diol to propionaldehyde by glycerol dehydrase, a coenzyme B12 dependent reaction, J. Am. Chem. Soc, 94, 275, 10.1021/ja00756a050

Zhao, 1992, Radical intermediates in the coenzyme B12dependent methylmalonyl-CoA mutase reaction shown by ESR spectroscopy, Angew. Chem. Int. Ed. Engl, 31, 215, 10.1002/anie.199202151

Zhao, 1994, Electron paramagnetic resonance studies of the methylmalonyl-CoA mutase reaction, Eur. J. Biochem, 225, 891, 10.1111/j.1432-1033.1994.0891b.x

Keep, 1993, The synthetic substrate succinyl(carbadethia)-CoA generates cob(II)alamin on adenosylcobalamin-dependent methylmalonyl-CoA mutase, Biochem. J, 295, 387, 10.1042/bj2950387

Rétey, 1964, The absolute configuration of methylmalonyl-CoA mutase, Biochem. Biophys. Res. Commun, 16, 358, 10.1016/0006-291X(64)90040-3

Eggerer, 1960, On the mechanism of the cobamide coenzyme dependent isomerization of methylmalonyl-CoA to succinyl-CoA, J. Am. Chem. Soc, 82, 1644, 10.1021/ja01495a064

Francalanci, 1986, The subunit structure of methylmalonyl-CoA mutase from Propionibacterium shermanii, Biochem. J, 236, 489, 10.1042/bj2360489

Marsh, 1989, Cloning and structural characterization of the genes coding for adenosylcobalamin-dependent methylmalonyl-CoA mutase from Propionibacterium shermanii, Biochem. J, 260, 345, 10.1042/bj2600345

Wölfle, 1986, On the mechanism of action of methylmalonyl-CoA mutase. Change of the steric course on isotopic substitution, Eur. J. Biochem, 156, 545, 10.1111/j.1432-1033.1986.tb09614.x

Keep, 1992, Studies on the structure and mechanism of methylmalonyl-CoA mutase. [PhD thesis]

Jansen, 1989, Cloning of full-length methylmalonyl-CoA mutase from a cDNA library using the polymerase chain reaction, Genomics, 4, 198, 10.1016/0888-7543(89)90300-5

Drennan, 1994, Cobalamin-dependent methionine synthase: the structure of a methylcobalamin-binding fragment and implications for other B12-dependent enzymes, Curr. Opin. Struct. Biol, 4, 919, 10.1016/0959-440X(94)90275-5

Drennan, 1994, How a protein binds B12: a 3.0 å X-ray structure of B12-binding domains of methionine synthase, Science, 266, 1669, 10.1126/science.7992050

Marsh, 1992, Cloning and sequencing of glutamate mutase component S from Clostridium tetanomorphum. Homologies with other cobalamin-dependent enzymes, FEBS Lett, 310, 167, 10.1016/0014-5793(92)81321-C

Padmakumar, 1995, Coenzyme B12 is coordinated by histidine and not by dimethylbenzimidazole on methylmalonyl-CoA mutase, J. Am. Chem. Soc, 117, 7033, 10.1021/ja00131a039

Brünger, 1993

Brändén, 1991, pp. 43, 48

Ito, 1991, Novel thioether bond revealed by a 1.7 å crystal structure of galactose oxidase, Nature, 350, 87, 10.1038/350087a0

Parsons, 1995, Crystal structure of a quinoenzyme: copper amine oxidase of Escherichia coli at 2 å resolution, Structure, 3, 1171, 10.1016/S0969-2126(01)00253-2

Picot, 1994, The crystal structure of the membrane protein prostaglandin H2 synthase-1, Nature, 367, 243, 10.1038/367243a0

Halpern, 1984, Cobalt–carbon bond dissociation energy of coenzyme B12, J. Am. Chem. Soc, 106, 8317, 10.1021/ja00338a065

Finke, 1984, Thermolysis of adenosylcobalamin: a product, kinetic and Co–C5′ bond dissociation study, Inorg. Chem, 23, 3041, 10.1021/ic00188a002

Dolphin, 1982

Vallee, 1968, Metalloenzymes: the entatic nature of their active sites, Proc. Natl. Acad. Sci. USA, 59, 498, 10.1073/pnas.59.2.498

Perutz, 1987, Stereochemistry of cooperative mechanisms in hemoglobin, Accounts Chem. Res, 20, 309, 10.1021/ar00141a001

McKie, 1990, Adenosylcobalamin-dependent methylmalonyl-CoA mutase from Propionibacterium shermanii. Active holoenzyme produced from Escherichia coli., Biochem J, 269, 293, 10.1042/bj2690293

Marsh, 1988, Crystallisation and preliminary diffraction data for adenosylcobalamin-dependent methylmalonyl-CoA mutase from Propionibacterium shermanii, J. Mol. Biol, 200, 421, 10.1016/0022-2836(88)90252-5

Teng, 1990, Mounting of crystals for macromolecular crystallography in a free-standing thin film, J. Appl. Cryst, 23, 387, 10.1107/S0021889890005568

Cosier, 1986, A nitrogen gas stream cryostat for general X-ray diffraction studies, J. Appl. Cryst, 19, 105, 10.1107/S0021889886089835

Leslie, 1992, Recent changes to the MOSFLM package for processing film and image plate data

Collaborative Computational Project No.4, 1994, The CCP4 suite: programs for protein crystallography, Acta Cryst. D, 50, 760, 10.1107/S0907444994003112

Sheldrick, 1991, Heavy atom location using SHELXS-90, 23

Otwinowski, 1991, Maximum likelihood refinement of heavy atom parameters, 80

Vellieux, 1995, DEMON/ANGEL: a suite of programs to carry out density modification, J. Appl. Cryst, 28, 347, 10.1107/S0021889894012355

Kleywegt, 1994, Halloween… masks and bones, 59

Navaza, 1994, AMoRe: an automated package for molecular replacement, Acta Cryst. A, 50, 157, 10.1107/S0108767393007597

Tickle, 1992, Fast Fourier translation functions, 20

Abrahams, 1996, Methods used in the structure determination of bovine mitochondrial F1 ATPase, Acta Cryst. D, 52, 30, 10.1107/S0907444995008754

Read, 1986, Improved Fourier coefficients for maps using phases from partial structures with errors, Acta Cryst. A, 42, 140, 10.1107/S0108767386099622

Jones, 1991, Improved methods for building protein models in electron density maps and the location of errors in these models, Acta Cryst. A, 47, 110, 10.1107/S0108767390010224

Tronrud, 1987, An efficient general-purpose least-squares refinement program for macromolecular structures, Acta Cryst. A, 43, 489, 10.1107/S0108767387099124

Konnert, 1980, A restrained-parameter thermal-factor refinement procedure, Acta Cryst. A, 36, 344, 10.1107/S0567739480000794

Kräutler, 1994, Direct evidence for the conformational distortion of the corrin ring by the nucleotide base in vitamin B12: synthesis and solution spectroscopic and crystal structure analysis of cob-cyanoimidazolylcobamide, Inorg. Chem, 33, 4128, 10.1021/ic00096a043

Kratky, 1995, Accurate structural data demystify B12: high resolution solid-state structure of aquocobalamin perchlorate and structural analysis of the aquocobalamin ion in solution, J. Am. Chem. Soc, 117, 456, 10.1021/ja00121a022

Kräutler, 1989, Coenzyme B12 chemistry: the crystal and molecular structure of cob(II)alamin, J. Am. Chem. Soc, 111, 8936, 10.1021/ja00206a037

Rossi, 1985, The structure of a B12 coenzyme: methylcobalamin studies by X-ray and NMR methods, J. Am. Chem. Soc, 107, 738, 10.1021/ja00292a046

Kraulis, 1991, MOLSCRIPT: a program to produce both detailed and schematic structures, J. Appl. Cryst, 24, 946, 10.1107/S0021889891004399

Nicholls, 1991, Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons, Proteins, 11, 281, 10.1002/prot.340110407