Spin-orbit coupling and zero-field splitting of the high-spin ferric enzyme-substrate complex： Protocatechuate 3,4-dioxygenase complexed with 3,4-dihydroxyphenylacetate

We used density functional calculations to investigate the electronic origins of the magnetic properties of the high-spin ferric en- zyme-substrate complex protocatechuate 3,4-dioxygenase （3,4-PCD）. The calculated g-tensors show that ligand-to-metal charge transfer transitions are from the protocate...

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Published inChinese science bulletin Vol. 58; no. 6; pp. 627 - 633
Main Authors Lü, LingLing, Zhu, YuanCheng, Wang, XiaoFang, Zuo, GuoFang, Guo, Feng, Zhao, SuRui, Wang, YongCheng
Format Journal Article
LanguageEnglish
Published Heidelberg Springer-Verlag 01.02.2013
SP Science China Press
Subjects
Charge transfer
Chemistry/Food Science
Earth Sciences
Electronics
Engineering
Humanities and Social Sciences
iron
Life Sciences
Magnetic properties
Mathematical analysis
multidisciplinary
Orbitals
Origins
oxygenases
phenolic acids
Physics
Science
Science (multidisciplinary)
Spin-orbit interactions
Splitting
原儿茶酸
双加氧酶
复合物
密度泛函计算
底物
自旋轨道耦合
零场分裂
高自旋
zero-field splitting
tensor
3,4-PCD-PCA
spin-orbit coupling
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Summary:We used density functional calculations to investigate the electronic origins of the magnetic properties of the high-spin ferric en- zyme-substrate complex protocatechuate 3,4-dioxygenase （3,4-PCD）. The calculated g-tensors show that ligand-to-metal charge transfer transitions are from the protocatechuate （PCA） and Tyr408 orbitals to the Fe dπ orbitals, which lead to x- and y-polarized transitions. These polarized transitions require a spin-orbit coupling （SOC） matrix element in the z-direction, Lz （z = z＇）, resulting in a gz＇ value of 2.0158, significantly deviating from 2.0023. A large zero-field splitting parameter value of ＋1.147 cm-1 is due to AS = -1 spin-orbit mixing with the quartet states for the sextet ground state, accounting for around 73% of the SOC contribution. The SOC matrix elements indicate that the high-spin d5 system Fe（III）, 3,4-PCD-PCA is a weak spin-crossover compound with an SOC of 31.56 cm-1.
Bibliography:3,4-PCD-PCA, g-tensor, zero-field splitting, spin-orbit coupling
11-1785/N
We used density functional calculations to investigate the electronic origins of the magnetic properties of the high-spin ferric en- zyme-substrate complex protocatechuate 3,4-dioxygenase （3,4-PCD）. The calculated g-tensors show that ligand-to-metal charge transfer transitions are from the protocatechuate （PCA） and Tyr408 orbitals to the Fe dπ orbitals, which lead to x- and y-polarized transitions. These polarized transitions require a spin-orbit coupling （SOC） matrix element in the z-direction, Lz （z = z＇）, resulting in a gz＇ value of 2.0158, significantly deviating from 2.0023. A large zero-field splitting parameter value of ＋1.147 cm-1 is due to AS = -1 spin-orbit mixing with the quartet states for the sextet ground state, accounting for around 73% of the SOC contribution. The SOC matrix elements indicate that the high-spin d5 system Fe（III）, 3,4-PCD-PCA is a weak spin-crossover compound with an SOC of 31.56 cm-1.
http://dx.doi.org/10.1007/s11434-012-5316-7
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:1001-6538
1861-9541
DOI:10.1007/s11434-012-5316-7