Dioxygen Binding and Sensing Proteins
نویسندگان
چکیده
منابع مشابه
Oxygen-binding and sensing proteins
This collection of papers is a snapshot of topics presented at the international conference on Oxygen-Binding and Sensing Proteins (O2BiP) held in Sheffield, UK, on 6 (th)-10 (th) July 2014. The collection will grow over time as new papers relating to O2BiP topics are completed and published.
متن کاملReply to Kiser: Dioxygen binding in NOV1 crystal structures.
In PNAS (1) Kiser has expressed some skepticism about the identity of the active-site dioxygen molecule and suggests that the density is better modeled with two water molecules at partial occupancy. In response, we have performed an extended analysis with the following results. There are currently 321 entries for proteins containing dioxygen (PDB OXY) in the Protein Data Bank (PDB). As might be...
متن کاملReversible dioxygen binding on asymmetric dinuclear rhodium centres.
Electron-deficient dinuclear rhodium complexes [Rh2Cl2(μ-dpmppp)(RNC)] (1), with the linear tetraphosphine ligand dpmppp, showed reversible binding of molecular oxygen to form asymmetric dirhodium η(2)-peroxo complexes [Rh2Cl2(O2)(μ-dpmppp)(RNC)] (2) stabilized by a Rh→Rh dative bond.
متن کاملReversible dioxygen binding in solvent-free liquid myoglobin.
The ensemble of forces that stabilize protein structure and facilitate biological function are intimately linked with the ubiquitous aqueous environment of living systems. As a consequence, biomolecular activity is highly sensitive to the interplay of solvent-protein interactions, and deviation from the native conditions, for example by exposure to increased thermal energy or severe dehydration...
متن کاملReappraisal of dioxygen binding in NOV1 crystal structures.
McAndrew et al. (1) report the crystal structure of NOV1, a stilbene-cleaving carotenoid cleavage oxygenase (CCO), in substrate-free and substrate/productbound forms, all of which with dioxygen (O2) bound to the nonheme iron center of the enzyme. In mononuclear nonheme iron enzymes studied to date, the Fe–O2 interaction is strongly promoted by the binding of organic substrate/cofactor at or nea...
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ژورنال
عنوان ژورنال: Antioxidants & Redox Signaling
سال: 2020
ISSN: 1523-0864,1557-7716
DOI: 10.1089/ars.2020.8034