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Volumn 15, Issue 6, 2009, Pages 1370-1376

Stereoselective hydrogenation of olefins using rhodium-substituted carbonic anhydrase - A new reductase

Author keywords

Carbonic anhydrase; Enzyme catalysis; Hydrogenation; Metalloenzymes; Protein modifications

Indexed keywords

BINDING SITES; CATALYSIS; CATALYST SELECTIVITY; ENZYME ACTIVITY; HYDROGEN; HYDROGENATION; LIGANDS; OLEFINS; REACTION KINETICS; RHODIUM; STEREOSELECTIVITY; SUBSTRATES; TRANSITION METALS;

EID: 60749117181     PISSN: 09476539     EISSN: 15213765     Source Type: Journal    
DOI: 10.1002/chem.200801673     Document Type: Article
Times cited : (88)

References (58)
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    • The Hmd class of hydrogenases use a cofactor. but hydrogen atoms still end up as protons in water: S. Shima, R. K. Thauer, Chem. Rec. 2007, 7, 37-46.
    • c) The Hmd class of hydrogenases use a cofactor. but hydrogen atoms still end up as protons in water: S. Shima, R. K. Thauer, Chem. Rec. 2007, 7, 37-46.
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    • the interest in the binding of these complexes to proteins stems from reports of their anti-cancer activity: J. L. Bear, H. B. Gray, L. Rainen, I. M. Chang, R. A. Howard, G. Serio, A. P. Kimball, Cancer Chemother. Rep. 1975, 159, 611-620
    • c) the interest in the binding of these complexes to proteins stems from reports of their anti-cancer activity: J. L. Bear, H. B. Gray, L. Rainen, I. M. Chang, R. A. Howard, G. Serio, A. P. Kimball, Cancer Chemother. Rep. 1975, 159, 611-620.
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    • a preliminary communication from this group (M. Marchetti. G. Mangano, S. Paganelli. C. Botteghi, Tetrahedron Lett. 2000, 41, 3717-3720) mentioned enantioselectivity for one substrate and selective hydroformylation of smaller aldehydes over larger ones, but this full paper did not confirm the preliminary report.
    • a preliminary communication from this group (M. Marchetti. G. Mangano, S. Paganelli. C. Botteghi, Tetrahedron Lett. 2000, 41, 3717-3720) mentioned enantioselectivity for one substrate and selective hydroformylation of smaller aldehydes over larger ones, but this full paper did not confirm the preliminary report.
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    • Zinc(II) has a radius of 0.74 Å, while rhodium(III) has a radius of 0.68 Å (CRC Handbook of Chemistry and Physics. 59th ed, 1978-1979, p. F-213). The ionic radius of rhodium(1) will be > 0.68 Â and likely similar to that for zinc(11).
    • Zinc(II) has a radius of 0.74 Å, while rhodium(III) has a radius of 0.68 Å (CRC Handbook of Chemistry and Physics. 59th ed, 1978-1979, p. F-213). The ionic radius of rhodium(1) will be > 0.68 Â and likely similar to that for zinc(11).
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    • We did not observe a color characteristic of the hybrid enzyme. Both [Rh-(cod)3]BF4 and bipyridine-[Rh] solutions are pale yellow and have indistinguishable UV/Vis spectra. Similarly, the hCAII 9*His-[Rh] complex shows a similar spectrum with an additional strong absorption at 280 nm due to protein
    • 4 and bipyridine-[Rh] solutions are pale yellow and have indistinguishable UV/Vis spectra. Similarly, the hCAII 9*His-[Rh] complex shows a similar spectrum with an additional strong absorption at 280 nm due to protein.
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    • X-ray structure: A. E. Eriksson, P. M. Kylsten, T A. Jones, A. Liljas, Proteins 1988, 4, 283-293. The Supporting Information includes a graphic showing the location of these histidines.
    • X-ray structure: A. E. Eriksson, P. M. Kylsten, T A. Jones, A. Liljas, Proteins 1988, 4, 283-293. The Supporting Information includes a graphic showing the location of these histidines.
  • 39
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    • Bovine CA II has no cysteine residues, but the human enzyme has one at position 206, which is buried. Site-directed mutagenesis suggested that it does not bind rhodium.
    • Bovine CA II has no cysteine residues, but the human enzyme has one at position 206, which is buried. Site-directed mutagenesis suggested that it does not bind rhodium.
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    • Wild-type hCAII and several variants precipitated after treatment with DEPC or after subsequent exchange of the zinc with rhodium. The triple mutant H4/10R, H17F was an exception since it retained 90% activity in the hydrolysis of 4-nitrophenyl acetate after treatment with DEPC and remained soluble after exchange of the zinc with rhodium
    • Wild-type hCAII and several variants precipitated after treatment with DEPC or after subsequent exchange of the zinc with rhodium. The triple mutant H4/10R + H17F was an exception since it retained 90% activity in the hydrolysis of 4-nitrophenyl acetate after treatment with DEPC and remained soluble after exchange of the zinc with rhodium.
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    • M and ftcat are difficult to measure accurately with the high pressure reaction chambers. For this reason, we focused on selectivity where we measure the relative, not absolute, amounts of products.
    • M and ftcat are difficult to measure accurately with the high pressure reaction chambers. For this reason, we focused on selectivity where we measure the relative, not absolute, amounts of products.
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    • X-ray structures of rhodium(1)-olefin complexes show Rh-C distances of approximately 2 Å: J. A. Evans. D. R. Russell, J. Chem. Soc. D 1971, 197-198.
    • X-ray structures of rhodium(1)-olefin complexes show Rh-C distances of approximately 2 Å: J. A. Evans. D. R. Russell, J. Chem. Soc. D 1971, 197-198.
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    • Pressure is not the cause of the unstability since the protein precipitates over several hours even under 1 atm of hydrogen
    • Pressure is not the cause of the unstability since the protein precipitates over several hours even under 1 atm of hydrogen.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.