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[HTML][HTML] Metalloproteins containing cytochrome, iron–sulfur, or copper redox centers
Redox reactions play important roles in almost all biological processes, including
photosynthesis and respiration, which are two essential energy processes that sustain all life …
photosynthesis and respiration, which are two essential energy processes that sustain all life …
Electron spin echo envelope modulation (ESEEM) spectroscopy as a tool to investigate the coordination environment of metal centers
The applications of electron spin echo envelope modulation (ESEEM) spectroscopy to study
paramagnetic metal centers in metalloproteins and bioinorganic complexes are reviewed …
paramagnetic metal centers in metalloproteins and bioinorganic complexes are reviewed …
The [Fe-Fe]-hydrogenase maturation protein HydF from Thermotoga maritima is a GTPase with an iron-sulfur cluster
X Brazzolotto, JK Rubach, J Gaillard… - Journal of Biological …, 2006 - jbc.org
The active site of [Fe-Fe]-hydrogenases is composed of a di-iron complex, where the two
metal atoms are bridged together by a putative di (thiomethyl) amine molecule and are also …
metal atoms are bridged together by a putative di (thiomethyl) amine molecule and are also …
The structures of Rieske and Rieske-type proteins
TA Link - Advances in Inorganic Chemistry, 1999 - Elsevier
Publisher Summary Over the past few decades, numerous studies of this so-called Rieske
protein have tried to unravel the molecular basis of its unusual properties. The …
protein have tried to unravel the molecular basis of its unusual properties. The …
HYSCORE and QM/MM Studies of Second Sphere Variants of the Type 1 Copper Site in Azurin: Influence of Mutations on the Hyperfine Couplings of Remote …
Secondary coordination sphere (SCS) interactions have been shown to play important roles
in tuning reduction potentials and electron transfer (ET) properties of the Type 1 copper …
in tuning reduction potentials and electron transfer (ET) properties of the Type 1 copper …
Binding of Histidine in the (Cys)3(His)1-Coordinated [2Fe−2S] Cluster of Human mitoNEET
MM Dicus, A Conlan, R Nechushtai… - Journal of the …, 2010 - ACS Publications
Human mitoNEET is a homodimeric iron− sulfur protein located in the outer mitochondrial
membrane with unknown function, but which is known to interact with thiazolidinedione …
membrane with unknown function, but which is known to interact with thiazolidinedione …
Probing the coordination and function of Fe4S4 modules in nitrogenase assembly protein NifB
NifB is an essential radical S-adenosylmethionine (SAM) enzyme for nitrogenase cofactor
assembly. Previous studies show that NifB couples a putative pair of [Fe4S4] modules …
assembly. Previous studies show that NifB couples a putative pair of [Fe4S4] modules …
[HTML][HTML] Advanced paramagnetic resonance spectroscopies of iron–sulfur proteins: Electron nuclear double resonance (ENDOR) and electron spin echo envelope …
The advanced electron paramagnetic resonance (EPR) techniques, electron nuclear double
resonance (ENDOR) and electron spin echo envelope modulation (ESEEM) spectroscopies …
resonance (ENDOR) and electron spin echo envelope modulation (ESEEM) spectroscopies …
Apd1 and Aim32 are prototypes of bishistidinyl-coordinated non-Rieske [2Fe–2S] proteins
K Stegmaier, CM Blinn, DF Bechtel… - Journal of the …, 2019 - ACS Publications
Apd1, a cytosolic yeast protein, and Aim32, its counterpart in the mitochondrial matrix, have
a C-terminal thioredoxin-like ferredoxin (TLF) domain and a widely divergent N-terminal …
a C-terminal thioredoxin-like ferredoxin (TLF) domain and a widely divergent N-terminal …
Axial solvent coordination in “base-off” cob (II) alamin and related Co (II)-corrinates revealed by 2D-EPR
Detailed information on the structure of cobalt (II) corrinates is of interest in the context of
studies on the coenzyme B12 catalyzed enzymatic reactions, where cob (II) alamin has been …
studies on the coenzyme B12 catalyzed enzymatic reactions, where cob (II) alamin has been …