Section D—Engineering

Blanchard, Arthur H.

doi:10.1126/science.45.1164.389

Cited by 1 publication

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“…The heme methyl lines of DvH cytochrome c 553 are particularly well resolved and were previously assigned at 296 K (Me1, 20.69 ppm; Me3, 23.40 ppm; Me5, 22.11 ppm and Me8, 30.70 ppm) [9]. The resonances of the cysteines bonded to the [4Fe-4S] cluster of DdN ferredoxin I were also previously assigned (C9L1, 11.25 ppm; C12L2, 16.87 ppm; C15L1, 16.08 ppm and C51L2, 11.69 ppm) [10].…”

Section: D Nmr Analysis Of the Complex Formationmentioning

confidence: 58%

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Mapping the cytochrome c₅₅₃ interacting site using ¹H and ¹⁵N NMR

Morelli

Guerlesquin

1999

FEBS Letters

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Cytochrome c 553 is the electron transfer partner of formate dehydrogenase and of [Fe]-hydrogenase, two metalloenzymes essential in the metabolism of sulfate reducing bacteria. These two enzymes contain a`ferredoxin-like' domain which presents 30% identity with Desulfovibrio desulfuricans Norway ferredoxin I. This was chosen as a model for the`ferredoxin-like' domain involved in the electron transfer reaction with cytochrome c 553 . 1D NMR titration of complex formation gave us the stoichiometry (1:1) and the dissociation constant of the complex (K d V V3U U10 36 M). 2D heteronuclear NMR experiments were performed to analyze the 1 H and 15 N chemical shift variations that are induced by the protein-protein recognition. This is the first mapping of the interaction site on a c-type cytochrome, using heteronuclear NMR.z 1999 Federation of European Biochemical Societies.

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Section: D Nmr Analysis Of the Complex Formationmentioning

confidence: 58%

“…15 N chemical shifts were referenced indirectly using the above 1 H reference and the gyromagnetic ratio (0.101329118) [8]. The 1 H and 15 N chemical shifts of oxidized cytochrome c 553 previously reported [7,9] were used for the resonance assignments in 1D and 2D experiments.…”

Section: Nmr Spectramentioning

confidence: 99%