FTIR studies of organometalcarbonyl-tagged enzymes

被引:17
作者
Anson, CE
Creaser, CS
Egyed, O
Stephenson, GR
机构
[1] NOTTINGHAM TRENT UNIV,DEPT CHEM & PHYS,NOTTINGHAM NG11 8NS,ENGLAND
[2] UNIV E ANGLIA,SCH CHEM SCI,NORWICH NR4 7TJ,NORFOLK,ENGLAND
[3] HUNGARIAN ACAD SCI,CENT RES INST CHEM,H-1525 BUDAPEST,HUNGARY
基金
英国工程与自然科学研究理事会; 英国生物技术与生命科学研究理事会;
关键词
infrared spectroscopy; proteins; spectroscopic probe; organometallic label;
D O I
10.1016/S1386-1425(97)00080-2
中图分类号
O433 [光谱学];
学科分类号
0703 ; 070302 ;
摘要
Attachment of organometaltricarbonyl tags to enzymes is revealed by changes in the vibrational modes of the carbonyl groups. Shoulders on nu(sym)(CO) and nu(asym)(CO) bands in the FTIR spectrum of an organometallic tag derived from tricarbonyl[1-{(2,3,4,5-eta)-2,4-cyclohexadien-1-yl}pyridinium]iron(1+) hexafluorophosphate(1-)were detected on binding to enzymes (alpha-chymotrypsin, ribonuclease A, alkaline phosphatase and a triacylglycerol lipase). By comparison with tagging reactions between the tricarbonyliron moiety and model compounds, the new spectral features were attributed to an iron complex covalently bonded to the NH2 groups of the amino acid residues of the enzymes. FTIR spectroscopy was used to monitor deprotonation of tagged amino groups on the enzyme surface. Interactions between the organometalcarbonyl tag and other side-chain groups of the amino acid residues were also investigated. (C) 1997 Elsevier Science B.V.
引用
收藏
页码:1867 / 1877
页数:11
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