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PUBMED FOR HANDHELDS

Journal Abstract Search

512 related items for PubMed ID: 14995196

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  • 4. Dynamic docking and electron transfer between Zn-myoglobin and cytochrome b(5).
    Liang ZX, Nocek JM, Huang K, Hayes RT, Kurnikov IV, Beratan DN, Hoffman BM.
    J Am Chem Soc; 2002 Jun 19; 124(24):6849-59. PubMed ID: 12059205
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  • 5. Evolving the [myoglobin, cytochrome b(5)] complex from dynamic toward simple docking: charging the electron transfer reactive patch.
    Trana EN, Nocek JM, Knutson AK, Hoffman BM.
    Biochemistry; 2012 Oct 30; 51(43):8542-53. PubMed ID: 23067206
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  • 6. Electrostatic redesign of the [myoglobin, cytochrome b5] interface to create a well-defined docked complex with rapid interprotein electron transfer.
    Xiong P, Nocek JM, Griffin AK, Wang J, Hoffman BM.
    J Am Chem Soc; 2009 May 27; 131(20):6938-9. PubMed ID: 19419145
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  • 8. Preparation of apo-cytochrome b5 utilizing heme transfer to apo-myoglobin.
    Mrazova B, Martinek V, Martinkova M, Sulc M, Frei E, Stiborova M.
    Neuro Endocrinol Lett; 2009 May 27; 30 Suppl 1():72-9. PubMed ID: 20027148
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  • 10. Interfacial hydration, dynamics and electron transfer: multi-scale ET modeling of the transient [myoglobin, cytochrome b5] complex.
    Keinan S, Nocek JM, Hoffman BM, Beratan DN.
    Phys Chem Chem Phys; 2012 Oct 28; 14(40):13881-9. PubMed ID: 22955681
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  • 11. Role of the heme propionates in the interaction of heme with apomyoglobin and apocytochrome b5.
    Hunter CL, Lloyd E, Eltis LD, Rafferty SP, Lee H, Smith M, Mauk AG.
    Biochemistry; 1997 Feb 04; 36(5):1010-7. PubMed ID: 9033390
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  • 12. [Study of electron transport in heme proteins. X. Effect of pH, ionic strength, and zinc ions and the rate of ferricytochrome c reduction by oxymyoglobin from swine heart].
    Postnikova GB, Tselikova SV, Sivozhelezov VS.
    Mol Biol (Mosk); 1992 Feb 04; 26(4):880-90. PubMed ID: 1331770
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  • 13. [Electron transfer in hemoproteins. VIII. Influence of ionic strength on the rate of reduction of ferricytochrome c by oxymyoglobin derivatives, chemically modified at histidine residues].
    Postnikova GB, Shliapnikova EA, Atanasov BP, Vol'kenshteĭn.
    Mol Biol (Mosk); 1982 Feb 04; 16(1):104-16. PubMed ID: 6280031
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  • 14. 13C NMR spectroscopic and X-ray crystallographic study of the role played by mitochondrial cytochrome b5 heme propionates in the electrostatic binding to cytochrome c.
    Rodríguez-Marañón MJ, Qiu F, Stark RE, White SP, Zhang X, Foundling SI, Rodríguez V, Schilling CL, Bunce RA, Rivera M.
    Biochemistry; 1996 Dec 17; 35(50):16378-90. PubMed ID: 8973214
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  • 15. Engineering out motion: introduction of a de novo disulfide bond and a salt bridge designed to close a dynamic cleft on the surface of cytochrome b5.
    Storch EM, Daggett V, Atkins WM.
    Biochemistry; 1999 Apr 20; 38(16):5054-64. PubMed ID: 10213608
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  • 16. The influence of mutation at Glu44 and Glu56 of cytochrome b5 on the protein's stabilization and interaction between cytochrome c and cytochrome b5.
    Qian W, Sun YL, Wang YH, Zhuang JH, Xie Y, Huang ZX.
    Biochemistry; 1998 Oct 06; 37(40):14137-50. PubMed ID: 9760250
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  • 17. Identification of the basic residues of cytochrome f responsible for electrostatic docking interactions with plastocyanin in vitro: relevance to the electron transfer reaction in vivo.
    Soriano GM, Ponamarev MV, Piskorowski RA, Cramer WA.
    Biochemistry; 1998 Oct 27; 37(43):15120-8. PubMed ID: 9790675
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  • 18. [Applicability of molecular electrostatic interaction models to describing ionic strength dependence of reaction rate between myoglobin and cytochrome c].
    Komarov IuE, Sivozhelezov VS, Postnikova GB.
    Biofizika; 1998 Oct 27; 43(1):16-25. PubMed ID: 9567172
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  • 19. Contribution of Electrostatics to the Kinetics of Electron Transfer from NADH-Cytochrome b5 Reductase to Fe(III)-Cytochrome b5.
    Kollipara S, Tatireddy S, Pathirathne T, Rathnayake LK, Northrup SH.
    J Phys Chem B; 2016 Aug 25; 120(33):8193-207. PubMed ID: 27059440
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