O
Otto Epp
Researcher at Max Planck Society
Publications - 29
Citations - 8293
Otto Epp is an academic researcher from Max Planck Society. The author has contributed to research in topics: Photosynthetic reaction centre & Erythrocruorin. The author has an hindex of 22, co-authored 29 publications receiving 8165 citations. Previous affiliations of Otto Epp include Munich University of Applied Sciences.
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Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3Å resolution
TL;DR: The molecular structure of the photosynthetic reaction centre from Rhodopseudomonas viridis has been elucidated using X-ray crystallographic analysis and the first description of the high-resolution structure of an integral membrane protein is presented.
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X-ray structure analysis of a membrane protein complex. Electron density map at 3 Å resolution and a model of the chromophores of the photosynthetic reaction center from Rhodopseudomonas viridis
TL;DR: In this paper, an atomic model of the prosthetic groups of the reaction center complex (4 bacteriochlorophyll b, 2 bacteriopheophytin b, 1 non-heme iron, 1 menaquinone, 4 heme groups) was built.
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The refined structure of the selenoenzyme glutathione peroxidase at 0.2-nm resolution.
TL;DR: A general picture of a minimal reaction mechanism, in good agreement with functional and structural data, is proposed and a reasonable model of glutathione binding is presented.
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Crystallographic refinement at 2.3 A resolution and refined model of the photosynthetic reaction centre from Rhodopseudomonas viridis.
TL;DR: The atomic model of the photosynthetic reaction centre from the purple bacterium Rhodopseudomonas viridis has been refined to an R-value of 0.193 at 2.3 A resolution, and a group of about 10 water molecules is bound near the binding site of the secondary quinone QB.
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Pigment-protein interactions in the photosynthetic reaction centre from Rhodopseudomonas viridis.
TL;DR: An X‐ray structure analysis of the photosynthetic reaction centre from the purple bacterium Rhodopseudomonas viridis provides structural details of the pigment‐binding sites that may help to understand why only one branch of pigments is active in the light‐driven electron transfer.