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Heinz Körner

Researcher at Karlsruhe Institute of Technology

Publications -  10
Citations -  974

Heinz Körner is an academic researcher from Karlsruhe Institute of Technology. The author has contributed to research in topics: Reductase & Nitrous-oxide reductase. The author has an hindex of 9, co-authored 10 publications receiving 949 citations.

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Phylogeny of the bacterial superfamily of Crp-Fnr transcription regulators: exploiting the metabolic spectrum by controlling alternative gene programs

TL;DR: The Crp-Fnr regulators stand out in responding to a broad spectrum of intracellular and exogenous signals such as cAMP, anoxia, the redox state, oxidative and nitrosative stress, nitric oxide, carbon monoxide, 2-oxoglutarate, or temperature.
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Nitrous oxide reductase from denitrifying Pseudomonas perfectomarina. Purification and properties of a novel multicopper enzyme.

TL;DR: Nitrous oxide reductase from the denitrifying bacterium Pseudomonas perfectomarina has been isolated and purified to homogeneity and several spectroscopically distinct forms of the enzyme were identified.
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Multiple transcription factors of the FNR family in denitrifying Pseudomonas stutzeri : characterization of four fnr‐like genes, regulatory responses and cognate metabolic processes

TL;DR: The multiplicity of FNR factors in P. stutzeri underlines the versatility of the FNR scaffold to serve for transcriptional regulation directed at anaerobic or nitrate‐activated metabolic processes.
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Enzyme diversity and mosaic gene organization in denitrification.

TL;DR: The biochemical investigation of denitrification has culminated in the description of the crystal structures of the two types of nitrite reductases, ancestor of energy-conserving enzymes of the heme-copper oxidase superfamily.
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Structural investigations of the CuA centre of nitrous oxide reductase from Pseudomonas stutzeri by site-directed mutagenesis and X-ray absorption spectroscopy.

TL;DR: A structural model for the CuA centre of N2O reductase has been generated on the basis of the atomic coordinates for the homologous domain of cytochrome c oxidase and incorporating the current results and previous spectroscopic data.