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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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21
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0016712154
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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
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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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0034612142
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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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26
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11144300443
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T. Ueno, M. Suzuki, T Goto. T. Matsumoto, K. Nagayama. Y. Watanabe, Angew. Chem. 2004, 116, 2581-2584;
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60749109896
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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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31
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33745905616
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b) A. Fernández-Gacio. A. Codina. J. Fastrez, O. Raint, P. Soumillon, ChemBioChem 2006, 7, 1013-1016.
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b) Y. Kidani, J. Hirose, H. Koike, J. Biochem. 1976, 79, 43-51;
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0026047767
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S. K. Nair, T. L. Calderone, D. W. Christianson, C. A. Fierke, J. Biol. Chem. 1991, 266, 17320-17325.
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37
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60749107858
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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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38
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0024218294
-
-
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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60749116705
-
-
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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40
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60749090404
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K. L. Gudiksen, I. Gitlin, J. Yang, A. R. Urbach, D. T. Moustakas, G. M. Whitesides. J. Am. Chem. Soc. 2004, 126, 4707-4714.
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Whitesides, G.M.6
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41
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-
60749090984
-
-
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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-
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42
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60749094589
-
-
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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43
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0026355919
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44
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60749096099
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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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60749137212
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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.
-
-
-
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