Ca 2+ as cofactor of the mitochondrial H + ‐translocating F 1 F O ‐ATP (hydrol)ase

التفاصيل البيبلوغرافية
العنوان: Ca 2+ as cofactor of the mitochondrial H + ‐translocating F 1 F O ‐ATP (hydrol)ase
المؤلفون: Alessandra Pagliarani, Salvatore Nesci
المصدر: Proteins: Structure, Function, and Bioinformatics. 89:477-482
بيانات النشر: Wiley, 2021.
سنة النشر: 2021
مصطلحات موضوعية: chemistry.chemical_classification, 0303 health sciences, Enzyme complex, Oligomycin, biology, ATP synthase, Chemistry, ATPase, 030302 biochemistry & molecular biology, Mitochondrion, Biochemistry, Cofactor, 03 medical and health sciences, chemistry.chemical_compound, Enzyme, Structural Biology, ATP hydrolysis, biology.protein, Biophysics, Molecular Biology, 030304 developmental biology
الوصف: The mitochondrial F1 FO -ATPase in the presence of the natural cofactor Mg2+ acts as the enzyme of life by synthesizing ATP, but it can also hydrolyze ATP to pump H+ . Interestingly, Mg2+ can be replaced by Ca2+ , but only to sustain ATP hydrolysis and not ATP synthesis. When Ca2+ inserts in F1 , the torque generation built by the chemomechanical coupling between F1 and the rotating central stalk was reported as unable to drive the transmembrane H+ flux within FO . However, the failed H+ translocation is not consistent with the oligomycin-sensitivity of the Ca2+ -dependent F1 FO -ATP(hydrol)ase. New enzyme roles in mitochondrial energy transduction are suggested by recent advances. Accordingly, the structural F1 FO -ATPase distortion driven by ATP hydrolysis sustained by Ca2+ is consistent with the permeability transition pore signal propagation pathway. The Ca2+ -activated F1 FO -ATPase, by forming the pore, may contribute to dissipate the transmembrane H+ gradient created by the same enzyme complex. This article is protected by copyright. All rights reserved.
تدمد: 1097-0134
0887-3585
DOI: 10.1002/prot.26040
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_________::5bfbd96c07dc91f504c6f0dc9c8988d1
https://doi.org/10.1002/prot.26040
Rights: OPEN
رقم الانضمام: edsair.doi...........5bfbd96c07dc91f504c6f0dc9c8988d1
قاعدة البيانات: OpenAIRE
الوصف
تدمد:10970134
08873585
DOI:10.1002/prot.26040