Spin cascade and doming in ferric hemes: Femtosecond X-ray absorption and X-ray emission studies
Spin cascade and doming in ferric hemes: Femtosecond X-ray absorption and X-ray emission studies
复制标题
三价铁血红素中的自旋级联和隆起:飞秒 X 射线吸收和 X 射线发射研究
DOI:
10.1073/pnas.2009490117
复制
发表时间:
2020
影响因子:
11.1
通讯作者:
M. Chergui
中科院分区:
文献类型:
--
作者:
C. Bacellar;D. Kinschel;G. Mancini;R. Ingle;J. Rouxel;O. Cannelli;C. Cirelli;G. Knopp;J. Szlachetko;F. Lima;S. Menzi;G. Pamfilidis;K. Kubicek;D. Khakhulin;W. Gawelda;A. Rodriguez;M. Biednov;C. Bressler;C. Arrell;Philip J. M. Johnson;C. Milne;M. Chergui
Significance The structure–function relationship in central to biology, while the structural dynamics are driven by electronic changes. Doming of ferrous heme proteins, which is central to the respiratory function of hemoglobin, ensues from populating high-spin states. However, for ferric heme proteins, doming was excluded. Here, we show that high-spin states are populated in photoexcited ferric cytochrome c, and we present evidence for doming. We also conclude that photo- or thermally activated doming occurs in a wide variety of ferric heme proteins, calling for a deeper understanding of its role in their respective functions. The structure–function relationship is at the heart of biology, and major protein deformations are correlated to specific functions. For ferrous heme proteins, doming is associated with the respiratory function in hemoglobin and myoglobins. Cytochrome c (Cyt c) has evolved to become an important electron-transfer protein in humans. In its ferrous form, it undergoes ligand release and doming upon photoexcitation, but its ferric form does not release the distal ligand, while the return to the ground state has been attributed to thermal relaxation. Here, by combining femtosecond Fe Kα and Kβ X-ray emission spectroscopy (XES) with Fe K-edge X-ray absorption near-edge structure (XANES), we demonstrate that the photocycle of ferric Cyt c is entirely due to a cascade among excited spin states of the iron ion, causing the ferric heme to undergo doming, which we identify. We also argue that this pattern is common to a wide diversity of ferric heme proteins, raising the question of the biological relevance of doming in such proteins.
登录
查看更多内容
DOI:
--
发表时间:
1987
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
Chance,MR;Campbell,BF;Hoover,R;Friedman,JM
通讯作者:
Friedman,JM
影响因子:
15
作者:
Maes, EM;Walker, FA;Czernuszewicz, RS
通讯作者:
Czernuszewicz, RS
影响因子:
2.9
作者:
Roberts,SA;Weichsel,A;Qiu,Y;Shelnutt,JA;Walker,FA;Montfort,WR
通讯作者:
Montfort,WR
影响因子:
2.9
作者:
Belikova, NA;Vladimirov, YA;Kagan, VE
通讯作者:
Kagan, VE
DOI:
10.1126/science.aam6203
发表时间:
2017-06-23
期刊:
Science (New York, N.Y.)
影响因子:
--
作者:
Mara MW;Hadt RG;Reinhard ME;Kroll T;Lim H;Hartsock RW;Alonso-Mori R;Chollet M;Glownia JM;Nelson S;Sokaras D;Kunnus K;Hodgson KO;Hedman B;Bergmann U;Gaffney KJ;Solomon EI
通讯作者:
Solomon EI