Real-Time Study of the Modification of the Peptide Bond by Atomic Calcium

被引：13

作者：

Kummer, Kurt ^{[1
,2
]}

Vyalikh, Denis V. ^{[1
]}

Blueher, Anja ^{[3
,4
]}

Sivkov, Victor ^{[5
]}

Maslyuk, Volodymyr V. ^{[6
]}

Bredow, Thomas ^{[7
]}

Mertig, Ingrid ^{[6
]}

Mertig, Michael ^{[3
,4
]}

Molodtsov, Serguei L. ^{[8
]}

机构：

[1] Tech Univ Dresden, Inst Festkorperphys, D-01062 Dresden, Germany

[2] European Synchrotron Radiat Facil, F-38043 Grenoble, France

[3] Tech Univ Dresden, Max Bergmann Zentrum Biomat, D-01062 Dresden, Germany

[4] Tech Univ Dresden, Inst Werkstoffwissensch, D-01062 Dresden, Germany

[5] Russian Acad Sci, Ural Div, Komi Sci Ctr, Syktyvkar 167982, Russia

[6] Univ Halle Wittenberg, Fachbereich Phys, D-06099 Halle, Germany

[7] Univ Bonn, Inst Phys & Theoret Chem, D-53115 Bonn, Germany

[8] European XFEL GmbH, D-22761 Hamburg, Germany

来源：

JOURNAL OF PHYSICAL CHEMISTRY B | 2011年 / 115卷 / 10期

关键词：

CRYSTALLINE SURFACE-LAYERS; RAY-INDUCED DECOMPOSITION; S-LAYER; PHOTOELECTRON-SPECTROSCOPY; MASS-SPECTROMETRY; PROTEIN LAYERS; GOLD; PHOTOEMISSION; XPS; MICROSCOPY;

D O I：

10.1021/jp109555j

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

Strong chemical interaction between bacterial surface protein layers and calcium atoms deposited in situ on top was revealed by means of photoemission spectroscopy. The interaction appears to mainly happen at the oxygen site of the peptide bonds and involves a large charge transfer from Ca 4s states into the peptide backbone. Chemical kinetics of this reaction was characterized using time-dependent valence band photoemission, and the reaction rate constant was determined.

引用

页码：2401 / 2407

页数：7

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