METAL CENTERS IN BIOLOGICAL SYSTEMS

生物系统中的金属中心

• 批准号: 2168662
• 负责人: THOMAS G. SPIRO
• 金额: $ 20.81万
• 依托单位: PRINCETON UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 1977
• 资助国家: 美国
• 起止时间: 1977-08-01 至 1995-03-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/2168662
• 关键词: Arthropoda; Mollusca; Raman spectrometry; X ray crystallography; carbonate dehydratase; cobalt; copper; electron transport; enzyme structure; ferredoxin; hemocyanin; ion transport; iron; mathematics; metal complex; metalloproteins; microorganism; molybdenum; monophenol monooxygenase; oxidation reduction reaction; protein structure function; rubredoxins; sulfite reductase; sulfur compounds; zinc

Molecular interactions in metalloproteins will be studied using resonance Raman (RR) spectroscopy as a probe of structure. Emphasis will be placed on iron-sulfur cluster, for which reliable assignments and force fields are under development. A computer modelling approach t the interpretation of Fe-S protein RR spectra is planned. The non-redox Fe-S proteins aconitase and dihydroxy acid dehydratases will be examined with a view to understanding the nature of enzyme-substrate interactions. The coupling of Fe-S cluster and siroheme chemistry in sulfite reductase will be probed. Molybdenum redox proteins will be studied to elucidate the structure of the active molybdopterin cofactor. Copper proteins will be examined in their reduced state using ultraviolet RR spectroscopy to utilize enhancement of bound ligand modes via metal->ligand charge transfer transitions.

将使用以下方法研究金属蛋白中的分子相互作用 共振拉曼（RR）光谱作为结构探针。 强调 将被放置在铁硫集群上，为此进行可靠的分配 和力场正在开发中。 计算机建模方法 计划对 Fe-S 蛋白 RR 谱进行解释。 非氧化还原 将检查 Fe-S 蛋白 乌头酸酶和二羟酸脱水酶 以了解酶底物的性质 互动。 Fe-S簇与西罗血红素化学的耦合 将探测亚硫酸盐还原酶。 钼氧化还原蛋白将 研究阐明了活性钼蝶呤辅因子的结构。 将使用以下方法在还原状态下检查铜蛋白 紫外 RR 光谱法利用结合配体模式的增强 通过金属->配体电荷转移跃迁。

项目成果

An investigation of hydrogenase I and hydrogenase II from Clostridium pasteurianum by resonance Raman spectroscopy. Evidence for a [2Fe-2S] cluster in hydrogenase I.

通过共振拉曼光谱研究巴氏梭菌的氢化酶 I 和氢化酶 II。

• 发表时间: 1987
• 期刊: The Journal of biological chemistry
• 作者: Macor,KA;Czernuszewicz,RS;Adams,MW;Spiro,TG
• 通讯作者: Spiro,TG

Resonance Raman spectra of three-iron centers in ferredoxins from Desulfovibrio gigas.

来自 Desulfovibrio gigas 的铁氧还蛋白三铁中心的共振拉曼光谱。

• 发表时间: 1981
• 期刊: The Journal of biological chemistry
• 作者: Johnson,MK;Hare,JW;Spiro,TG;Moura,JJ;Xavier,AV;LeGall,J
• 通讯作者: LeGall,J

63/65Cu and 1/2H2O isotope shifts in the low-temperature resonance Raman spectrum of fungal laccase.

真菌漆酶低温共振拉曼光谱中的 63/65Cu 和 1/2H2O 同位素位移。

• DOI: 10.1016/0167-4838(86)90068-3
• 发表时间: 1986
• 期刊: Biochimica et biophysica acta
• 作者: Nestor,L;Reinhammar,B;Spiro,TG
• 通讯作者: Spiro,TG

Resonance Raman studies of Escherichia coli sulfite reductase hemoprotein. 2. Fe4S4 cluster vibrational modes.

大肠杆菌亚硫酸盐还原酶血红蛋白的共振拉曼研究。

• DOI: 10.1021/bi00439a023
• 发表时间: 1989
• 期刊: Biochemistry
• 影响因子: 2.9
• 作者: Madden,JF;Han,SH;Siegel,LM;Spiro,TG
• 通讯作者: Spiro,TG

Resonance Raman studies of Escherichia coli sulfite reductase hemoprotein. 1. Siroheme vibrational modes.

大肠杆菌亚硫酸盐还原酶血红蛋白的共振拉曼研究。

• DOI: 10.1021/bi00439a022
• 发表时间: 1989
• 期刊: Biochemistry
• 影响因子: 2.9
• 作者: Han,SH;Madden,JF;Thompson,RG;Strauss,SH;Siegel,LM;Spiro,TG
• 通讯作者: Spiro,TG