XFEL Crystal Structures of Peroxidase Compound II.
XFEL Crystal Structures of Peroxidase Compound II.
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DOI：
10.1002/anie.202103010
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发表时间：
2021-06-21
期刊：
影响因子：
--
通讯作者：
Moody PCE
中科院分区：
文献类型：
--
作者：
Kwon H;Basran J;Pathak C;Hussain M;Freeman SL;Fielding AJ;Bailey AJ;Stefanou N;Sparkes HA;Tosha T;Yamashita K;Hirata K;Murakami H;Ueno G;Ago H;Tono K;Yamamoto M;Sawai H;Shiro Y;Sugimoto H;Raven EL;Moody PCE
所有血红素酶中的氧活化需要形成高氧化态的铁，通常称为铁基血红素。有两种已知的中间体：化合物I和化合物II。铁基血红素的性质-以及它是FeIV=O还是FeIV‐OH物种-对于控制血红素酶的反应性非常重要。化合物I的最新证据表明铁基血红素是未质子化的FeIV=O物质。对于化合物II，铁基血红素的性质没有明确确定。在这里，我们报告了在SACLA使用X射线自由电子激光器收集的细胞色素c过氧化物酶（CcP）和抗坏血酸过氧化物酶（APX）中化合物II中间体的1.06μ m和1.50μ m晶体结构。 结构揭示了两种过氧化物酶之间的差异。CcP中的铁氧键长（1.76 π）明显短于APX（1.87 π）。 结果表明，在密切相关的过氧化物酶中，铁基种类在化合物I和化合物II种类之间被精细调节。我们认为这种微调与质子输送到血红素的功能需求有关。血红素反应性的酶促微调：两种不同的含血红素过氧化物酶-细胞色素c过氧化物酶和抗坏血酸过氧化物酶-的自由电子激光晶体结构显示铁基物种的性质存在差异。涉及结构相似的血红素活性位点内的精确酶促微调。
Oxygen activation in all heme enzymes requires the formation of high oxidation states of iron, usually referred to as ferryl heme. There are two known intermediates: Compound I and Compound II. The nature of the ferryl heme—and whether it is an FeIV=O or FeIV‐OH species—is important for controlling reactivity across groups of heme enzymes. The most recent evidence for Compound I indicates that the ferryl heme is an unprotonated FeIV=O species. For Compound II, the nature of the ferryl heme is not unambiguously established. Here, we report 1.06 Å and 1.50 Å crystal structures for Compound II intermediates in cytochrome c peroxidase (CcP) and ascorbate peroxidase (APX), collected using the X‐ray free electron laser at SACLA. The structures reveal differences between the two peroxidases. The iron‐oxygen bond length in CcP (1.76 Å) is notably shorter than in APX (1.87 Å). The results indicate that the ferryl species is finely tuned across Compound I and Compound II species in closely related peroxidase enzymes. We propose that this fine‐tuning is linked to the functional need for proton delivery to the heme. Enzymatic fine‐tuning of heme reactivity: Free‐electron laser crystal structures of two different heme‐containing peroxidases—cytochrome c peroxidase and ascorbate peroxidase—show differences in the nature of the ferryl species. Precise enzymatic fine‐tuning within structurally similar heme active sites is implicated.
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影响因子：
4.6
作者：
Gordon, Zachary;Drummond, Michael J.;Fout, Alison R.
通讯作者：
Fout, Alison R.
DOI：
10.1098/rspb.1937.0015
发表时间：
1937-04-01
期刊：
PROCEEDINGS OF THE ROYAL SOCIETY SERIES B-BIOLOGICAL SCIENCES
影响因子：
--
作者：
Keilin, D;Mann, T
通讯作者：
Mann, T
DOI：
10.1073/pnas.1521664113
发表时间：
2016-02-02
影响因子：
11.1
作者：
Chreifi, Georges;Baxter, Elizabeth L.;Poulos, Thomas L.
通讯作者：
Poulos, Thomas L.
DOI：
10.1107/s2059798316016314
发表时间：
2017-02-01
期刊：
Acta crystallographica. Section D, Structural biology
影响因子：
--
作者：
Kwon H;Smith O;Raven EL;Moody PC
通讯作者：
Moody PC
影响因子：
64.8
作者：
GEORGE, P
通讯作者：
GEORGE, P