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首页> 外文期刊>Biochemistry >Resonance Raman Spectra of Five-Coordinate Heme-Nitrosyl Cytochromes c ': Effect of the Proximal Heme-NO Environment
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Resonance Raman Spectra of Five-Coordinate Heme-Nitrosyl Cytochromes c ': Effect of the Proximal Heme-NO Environment

机译：五坐标血红素亚亚硝基亚胞嘧啶C'的共振拉曼光谱：近端血红素的影响

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摘要

Five-coordinate heme nitrosyl complexes (5cNO) underpin biological heme-NO signal transduction. Bacterial cytochromes c' are some of the few structurally characterized 5cNO proteins, exhibiting a distal to proximal 5cNO transition of relevance to NO sensing. Establishing how 5cNO coordination (distal vs proximal) depends on the heme environment is important for understanding this process. Recent 5cNO crystal structures of Alcaligenes xylosoxidans cytochrome c' (AXCP) and Shewanella frigidimarina cytochrome c' (SFCP) show a basic residue (Arg124 and Lys126, respectively) near the proximal NO binding sites. Using resonance Raman (RR) spectroscopy, we show that structurally characterized 5cNO complexes of AXCP variants and SFCP exhibit a range of ?(NO) (1651-1671 cm(-1)) and nu(FeNO) (519-536 cm(-1)) vibrational frequencies, depending on the nature of the proximal heme pocket and the sample temperature. While the AXCP Arg124 residue appears to have little impact on 5cNO vibrations, the nu(NO) and nu(FeNO) frequencies of the R124K variant are consistent with (electrostatically) enhanced Fe(II) -> (NO)pi* backbonding. Notably, RR frequencies for SFCP and R124A AXCP are significantly displaced from the backbonding trendline, which in light of recent crystallographic data and density functional theory modeling may reflect changes in the Fe-N-O angle and/or extent of s-donation from the NO(pi*) to the Fe(II) (d(z)(2)) orbital. For R124A AXCP, correlation of vibrational and crystallographic data is complicated by distal and proximal 5cNO populations. Overall, this study highlights the complex structure-vibrational relationships of 5cNO proteins that allow RR spectra to distinguish 5cNO coordination in certain electrostatic and steric environments.
机译：五坐标血红素亚硝基络合物（5CNO）基础生物血红素 - 无信号转导。细菌细胞色素C'是一些结构表征的5CNO蛋白中的一些，表现出与不感测的相关性的远端5CNO转变。建立5CNO协调（远端VS近端）如何取决于HEME环境对于了解这一过程非常重要。最近的5CNO晶体结构的唑苯胺苯甲酰氧化酯细胞色素C'（AXCP）和鞘蛋白硫胺氨基堇细胞色素C'（SFCP）在近端没有结合位点附近显示碱基残基（ARC124和Lys126）。使用共振拉曼（RR）光谱学，我们表明，结构表征了AXCP变体和SFCP的5CNO复合物，表现出一系列？（NO）（1651-1671cm（-1））和Nu（FENO）（519-536cm（ - 1））振动频率，取决于近端血红素口袋的性质和样品温度。虽然AXCP ARG124残留物对5CNO振动影响很小，但R124K变体的NU（NO）和NU（FENO）频率与（静电）增强Fe（II） - >（NO）PI *答案一致。值得注意的是，SFCP和R124A AXCP的RR频率从后透趋势下显着置换，这在最近的晶体数据和密度函数理论建模可能反映了FE-NO角度和/或来自NO的S捐赠程度的变化（ pi *）到Fe（II）（D（Z）（2））轨道。对于R124A AXCP，振动和晶体数据的相关性通过远端和近端5CNO群体复杂化。总体而言，该研究突出了5CNO蛋白的复杂结构振动关系，其允许RR光谱区分在某些静电和空间环境中的5CNO协调。

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  • 来源
    《Biochemistry》 |2015年第21期|共8页
  • 作者

    Servid Amy E.; McKay Alison L.; Davis Cherry A.; Garton Elizabeth M.; Manole Andreea; Dobbin Paul S.; Hough Michael A.; Andrew Colin R.;

  • 作者单位

    Eastern Oregon Univ Dept Chem &

    Biochem La Grande OR 97850 USA;

    Eastern Oregon Univ Dept Chem &

    Biochem La Grande OR 97850 USA;

    Eastern Oregon Univ Dept Chem &

    Biochem La Grande OR 97850 USA;

    Eastern Oregon Univ Dept Chem &

    Biochem La Grande OR 97850 USA;

    Univ Essex Sch Biol Sci Colchester CO4 3SQ Essex England;

    Univ Essex Sch Biol Sci Colchester CO4 3SQ Essex England;

    Univ Essex Sch Biol Sci Colchester CO4 3SQ Essex England;

    Eastern Oregon Univ Dept Chem &

    Biochem La Grande OR 97850 USA;

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  • 正文语种 eng
  • 中图分类 生物化学;
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