FEBS Letters | |
Modelling heme d 1 | |
Andersson, Laura A.2  Chang, Chi K.3  Wu, Weishih3  Timkovich, Russell1  Loehr, Thomas M.2  | |
[1] Department of Chemistry, University of Alabama, University, AL 35486, USA;Department of Chemical and Biological Sciences, Oregon Graduate Institute, Beaverton, OR 97006-1999, USA;Department of Chemistry, Michigan State University, East Lansing, MI 48824 USA | |
关键词: Nitrite reductase; Pseudomonas aeruginosa; Heme d 1; Resonance Raman; Porphyrin; Saturated porphyrin; Hydroporphyrin; iBC; isobacteriochlorin; RR; resonance Raman; FTIR; Fourier transform infrared; TME; tetramethylester; Cu-d 1; the copper(II) TME of P. aeruginosa heme d 1; THP; tetrahydroporphyrin; | |
DOI : 10.1016/0014-5793(90)80946-G | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
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【 摘 要 】
The heme d 1 macrocycle of Ps. aeruginosa dissimilatory nitrite reductase is an iron porphyrin-3,8-dione with a 17-acrylate substituent. We have compared the RR properties of Cu-d 1, the copper(II) TME of extracted heme d 1, with those of models that differ only with respect to the acrylate: Cu-17-acrylate-mesoporphyrin-3,8-dione (2) and Cu-mesoporphyrin-3,8-dione (3). The RR spectrum of Cu-d 1 is very similar to that of 2, including v(C=O) at ~ 1720 cm−1. Replacement of the acrylate with propionate changes the spectrum markedly. For example, the v(C=O) mode of 3 shifts to 1712 cm−1, and peaks of Cu-d 1 and 2 at ~ 1400 and ~ 1535 cm−1 are shifted or absent from the spectrum of 3. FTIR spectra of 2 and 3 also differ in their νoxo(C=O) frequencies. The acrylate thus has a surprisingly strong influence on the electronic structural and spectral properties of heme d 1. These data provide a foundation for studies of the novel biological porphyrindione macrocycles.
【 授权许可】
Unknown
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