Intrinsic Property of Flavin Mononucleotide Controls its Optical Spectra in Three Redox States

被引：10

作者：

Ai, Yue-jie ^{[2
]}

Tian, Guangjun ^{[2
]}

Liao, Rong-zhen ^{[3
]}

Zhang, Qiong ^{[2
]}

Fang, Wei-hai ^{[1
]}

Luo, Yi ^{[2
,4
]}

机构：

[1] Beijing Normal Univ, Coll Chem, Beijing 100875, Peoples R China

[2] Royal Inst Technol, Sch Biotechnol, S-10691 Stockholm, Sweden

[3] Stockholm Univ, Dept Organ Chem, S-10691 Stockholm, Sweden

[4] Univ Sci & Technol China, Heifei Natl Lab Phys Sci Microscale, Hefei 230026, Anhui, Peoples R China

来源：

CHEMPHYSCHEM | 2011年 / 12卷 / 16期

关键词：

density functional calculations; flavin mononucleotides; flavodoxins; redox chemistry; vibrational resolved spectroscopy; DENSITY-FUNCTIONAL THEORY; CONFORMATIONAL DYNAMICS; FLAVODOXIN; OXIDATION; MOLECULES;

D O I：

10.1002/cphc.201100663

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：

Self-centered flavins: The actual profiles of optical spectra for flavin mononucleotide (FMN, see picture) were calculated using first-principles methods with the inclusion of vibration progressions. An excellent agreement with the experimental spectra shows that while specific short-range interactions are negligible in the determination of the optical spectra of FMN in three different redox states, the natural structures and intrinsic electronic excitations play an important role. Copyright © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

引用

页码：2899 / 2902

页数：4

共 19 条

[11] A microscopic view of miniprotein folding: Enhanced folding efficiency through formation of an intermediate
Neuweiler, H
Doose, S
Sauer, M
[J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2005, 102 (46) : 16650 - 16655
[12] Flavodoxins: sequence, folding, binding, function and beyond
Sancho, J
[J]. CELLULAR AND MOLECULAR LIFE SCIENCES, 2006, 63 (7-8) : 855 - 864
[13] Quantum Chemical Studies of Proton-Coupled Electron Transfer in Metalloenzymes
Siegbahn, Per E. M.
Blomberg, Margareta R. A.
[J]. CHEMICAL REVIEWS, 2010, 110 (12) : 7040 - 7061
[14] SIMONDSEN RP, 1980, MOL CELL BIOCHEM, V33, P13
[15] Ultrafast spectroscopy reveals subnanosecond peptide conformational dynamics and validates molecular dynamics simulation
Spörlein, S
Carstens, H
Satzger, H
Renner, C
Behrendt, R
Moroder, L
Tavan, P
Zinth, W
Wachtveitl, J
[J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2002, 99 (12) : 7998 - 8002
[16] Quantum mechanical continuum solvation models
Tomasi, J
Mennucci, B
Cammi, R
[J]. CHEMICAL REVIEWS, 2005, 105 (08) : 2999 - 3093
[17] COMPARISON OF THE CRYSTAL-STRUCTURES OF A FLAVODOXIN IN ITS 3 OXIDATION-STATES AT CRYOGENIC TEMPERATURES
WATT, W
TULINSKY, A
SWENSON, RP
WATENPAUGH, KD
[J]. JOURNAL OF MOLECULAR BIOLOGY, 1991, 218 (01) : 195 - 208
[18] Protein conformational dynamics probed by single-molecule electron transfer
Yang, H
Luo, GB
Karnchanaphanurach, P
Louie, TM
Rech, I
Cova, S
Xun, LY
Xie, XS
[J]. SCIENCE, 2003, 302 (5643) : 262 - 266
[19] A theoretical study of the structures of flavin in different oxidation and protonation states
Zheng, YJ
Ornstein, RL
[J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1996, 118 (39) : 9402 - 9408

← 1 2 →