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Volumn 16, Issue 36, 2010, Pages 11012-11019

Ketone-alcohol hydrogen-transfer equilibria: Is the biooxidation of halohydrins blocked?

Author keywords

Computational chemistry; Enzyme catalysis; Halohydrins; Hydrogen transfer; Ir spectroscopy

Indexed keywords

2-PROPANOL; ACTIVE SITE; ALCOHOL DEHYDROGENASE; BIO-OXIDATION; CARBONYL COMPOUNDS; CARBONYL GROUPS; DEGREE OF CONVERSION; ELECTRON WITHDRAWING GROUP; ELECTROPHILICITY; ENZYMATIC REDUCTION; ENZYME CATALYSIS; G-VALUES; GENERAL METHOD; HALOHYDRINS; HYDROGEN ACCEPTOR; HYDROGEN TRANSFER; INITIAL RATE; IR ABSORPTION; IR SPECTROSCOPY; ISODESMIC; KINETIC EFFECT; LACTOBACILLUS BREVIS; MEERWEIN-PONNDORF-VERLEY-OPPENAUER; OXIDATION OF ALCOHOLS; REDOX EQUILIBRIUM; REDOX TRANSFORMATIONS; REDUCTION PROCESS; THEORETICAL APPROACH; THERMODYNAMIC CONTROL; TRANSFER EQUILIBRIUM;

EID: 77956953927     PISSN: 09476539     EISSN: 15213765     Source Type: Journal    
DOI: 10.1002/chem.201001233     Document Type: Article
Times cited : (39)

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    • 3. We have also performed the enzymatic reactions coupling of 1c/2c with 2h/1h, respectively, obtaining similar results to the transformations shown in Scheme 2
    • 3. We have also performed the enzymatic reactions coupling of 1c/2c with 2h/1h, respectively, obtaining similar results to the transformations shown in Scheme 2.
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    • This is due to the fact that after 24 h the activity of LBADH and the effective concentration of NADP(H) considerably decrease (data not shown)
    • This is due to the fact that after 24 h the activity of LBADH and the effective concentration of NADP(H) considerably decrease (data not shown).
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.