Cu(I) recognition via cation-π and methionine interactions in CusF
نویسندگان
چکیده
منابع مشابه
Cation–π–cation interactions in structural biology
Biological structures are stabilized by a variety of noncovalent interactions, such as hydrogen bonds, π –stacking, salt bridges or hydrophobic interactions. Besides hydrogen bonds and π– stacking, cation–π interactions between aromatic rings and positively charged groups have emerged as one of the most important interactions in structural biology. Although the role and energetic characteristic...
متن کاملAdditivity of Cation-π Interactions: An ab Initio Computational Study on π-Cation-π Sandwich Complexes
Center for Drug DiscoVery and Design, State Key Laboratory of New Drug Research, Shanghai Institute of Materia Medica, Shanghai Institutes of Biological Sciences, Chinese Academy of Sciences, 555 Zu Chong Zhi Road, Shanghai, 201203, P. R. China, Technology Centre for Life Sciences, Singapore Polytechnic, 500 DoVer Road, Singapore 139651, Department of Neurobiology, Weizmann Institute of Science...
متن کاملEffects of Structure and Partially Localization of the π Electron Clouds of Single-Walled Carbon Nanotubes on the Cation-π Interactions
A C102H30 graphene sheet has been rolled up to construct Single-Walled Carbon NanoTube Fragments (SWCNTFs) as parts of armchair carbon nanotubes by computational quantum chemistry methods. Non-covalent cation-π interactions of the Na+ cation on the central rings of SWCNTFs have investigated. The binding energies of the Na+-SWCNTF complexes versus ...
متن کاملCation–π Interactions Contribute to Substrate Recognition in γ‐Butyrobetaine Hydroxylase Catalysis
γ-Butyrobetaine hydroxylase (BBOX) is a non-heme Fe(II) - and 2-oxoglutarate-dependent oxygenase that catalyzes the stereoselective hydroxylation of an unactivated C-H bond of γ-butyrobetaine (γBB) in the final step of carnitine biosynthesis. BBOX contains an aromatic cage for the recognition of the positively charged trimethylammonium group of the γBB substrate. Enzyme binding and kinetic anal...
متن کاملCH/π Interactions in Carbohydrate Recognition.
Many carbohydrate-binding proteins contain aromatic amino acid residues in their binding sites. These residues interact with carbohydrates in a stacking geometry via CH/π interactions. These interactions can be found in carbohydrate-binding proteins, including lectins, enzymes and carbohydrate transporters. Besides this, many non-protein aromatic molecules (natural as well as artificial) can bi...
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ژورنال
عنوان ژورنال: Nature Chemical Biology
سال: 2007
ISSN: 1552-4450,1552-4469
DOI: 10.1038/nchembio.2007.57