Studies of the heme components of cytochrome c oxidase by EPR spectroscopy von Van Gelder, Bob F., Beinert, Helmut

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Metallo-selective anti-mesoporphyrin antibodies von Hofstee, Paul J.M., Roozemond, Rob C., van Gelder, Bob F.

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An EPR study of the photodissociation reactions of oxidised cytochrome c oxidase-nitric oxide complexes von Boelens, Rolf, Wever, Ron, Van Gelder, Bob F., Rademaker, Henk

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Bovine cytochrome c oxidases, purified from heart, skeletal muscle, liver and kidney, differ in the small subunits but show the same reaction kinetics with cytochrome c von Sinjorgo, Karin M.C., Durak, Ilker, Dekker, Henk L., Edel, Cees M., Hakvoort, Theo B.M., van Gelder, Bob F., Muijsers, Anton O.

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The cytochrome c oxidase-azide-nitric oxide complex as a model for the oxygen-binding site von Boelens, Rolf, Rademaker, Henk, Wever, Ron, Van Gelder, Bob F.

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Isoforms of human cytochrome-c oxidase : subunit composition and steady-state kinetic properties von VAN KUILENBURG, A. B. P, DEKKER, H. L, VAN DEN BOGERT, C, NIEBOER, P, VAN GELDER, B. F, MUIJSERS, A. O

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Biochemical and biophysical studies on cytochrome aa3. VI. Reaction of cyanide with oxidized and reduced enzyme von Van Buuren, Karel J.H., Nicholls, Peter, Van Gelder, Bob F.

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Human hemi-myeloperoxidase : initial chlorinating activity at neutral pH, compound II and III formation, and stability towards hypochlorous acid and high temperature von ZUURBIER, K. W. M, VAN DEN BERG, J. D, VAN GELDER, B. F, MUIJSERS, A. O

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PRESTEADY-STATE AND STEADY-STATE KINETIC-PROPERTIES OF HUMAN CYTOCHROME-C-OXIDASE - IDENTIFICATION OF RATE-LIMITING STEPS IN MAMMALIAN CYTOCHROME-C-OXIDASE von VANKUILENBURG, ABP, GORREN, ACF, DEKKER, HL, NIEBOER, P, VANGELDER, BF, MUIJSERS, AO

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[10] Preparation of cytochrome oxidase from beef heart von Hartzell, Charles R., Beinert, Helmut, van Gelder, Bob F., King, Tsoo E.

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Biochemical and biophysical studies on cytochrome aa3: VIII. Effect of cyanide on the catalytic activity von Nicholls, Peter, Van Buuren, Karel J.H., Van Gelder, Bob F.

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The pre-steady state reaction of ferrocytochrome c with the cytochrome c-cytochrome aa3 complex von Veerman, Enno C.I., Wilms, Jan, Casteleijn, Gerard, Van Gelder, Bob F.

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Separation of enzymically active bovine cytochrome c oxidase monomers and dimers by high performance liquid chromatography von Hakvoort, Theo B.M., Sinjorgo, Karin M.C., Van Gelder, Bob F., Muijsers, Anton O.

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Biochemical and biophysical studies on cytochrome aa3. V. Binding of cyanide to cytochrome aa3 von Van Buuren, Karel J.H., Zuurendonk, Peter F., Van Gelder, Bob F., Muijsers, Anton O.

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A Spectroscopic Study of Nitric‐Oxide‐Treated Ceruloplasmin von LEEUWEN, François X. R., GELDER, Bob F.

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Biochemical and biophysical studies on cytochrome aa3 von Nicholls, Peter, Van Buuren, Karel J.H., Van Gelder, Bob F.

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The reactivity of thiol groups in bovine heart cytochrome c oxidase towards 5,5′-dithiobis(2-nitrobenzoic acid) von Verheul, Frans E.A.M., Draijer, J.Wim, Muijsers, Anton O., Van Gelder, Bob F.

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The mechanism of reduction of cytochrome c as studied by pulse radiolysis von Wilting, Jaap, Van Buuren, Karel J.H., Braams, Reinier, Van Gelder, Bob F.

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binding of carbon monoxide to cytochrome c oxidase von Wever, R, Drooge, J.H. van, Muijsers, A.O, Bakker, E.P, Gelder, B.F. van

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The mechanism of reduction of cytochrome c as studied by pulse radiolysis von Wilting, Jaap, Buuren, Karel J.H. van, Braams, R, Gelder, Bob F. van

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