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Auflistung nach Schlagwort "enzyme structure"

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Carbonic anhydrase subunits form a matrix-exposed domain attached to the membrane arm of mitochondrial complex I in plants

Sunderhaus, Stephanie; Dudkina, Natalya V.; Jänsch, Lothar; Klodmann, Jennifer; Heinemeyer, Jesco; Perales, Mariano; Zabaleta, Eduardo; Boekema, Egbert J.; Braun, Hans-Peter (Bethesda, Md. : ASBMB Publications, 2006)

Complex I of Arabidopsis includes five structurally related subunits representing γ-type carbonic anhydrases termed CA1, CA2, CA3, CAL1, and CAL2. The position of these subunits within complex I was investigated. Direct ...
The Oxidative Phosphorylation system of the mitochondria in plants

Braun, Hans-Peter (Amsterdam [u.a.] : Elsevier Science, 2020)

Mitochondrial Oxidative Phosphorylation (OXPHOS) provides ATP for driving cellular functions. In plants, OXPHOS takes place in the context of photosynthesis. Indeed, metabolism of mitochondria and chloroplasts is tightly ...
Structural Basis for Regulation of the Opposing (p)ppGpp Synthetase and Hydrolase within the Stringent Response Orchestrator Rel

Pausch, Patrick; Abdelshahid, Maha; Steinchen, Wieland; Schäfer, Heinrich; Gratani, Fabio Lino; Freibert, Sven-Andreas.; Wolz, Christiane; Turgay, Kürşad; Wilson, Daniel N.; Bange, Gert (New York, NY : Elsevier, 2020)

The stringent response enables metabolic adaptation of bacteria under stress conditions and is governed by RelA/SpoT Homolog (RSH)-type enzymes. Long RSH-type enzymes encompass an N-terminal domain (NTD) harboring the ...
A structural model of the cytochrome c reductase/oxidase supercomplex from yeast mitochondria

Heinemeyer, Jesco; Braun, Hans-Peter; Boekema, Egbert J.; Kouřil, Roman (Bethesda, Md. : ASBMB Publications, 2007)

Mitochondrial respiratory chain complexes are arranged in supercomplexes within the inner membrane. Interaction of cytochrome c reductase (complex III) and cytochrome c oxidase (complex IV) was investigated in Saccharomyces ...
Studies with lysine N6-hydroxylase. Effect of a mutation in the assumed FAD binding site on coenzyme affinities and on lysine hydroxylating activity

Stehr, Matthias; Smau, Liliana; Singh, Mahavir; Seth, Oliver; Macheroux, Peter; Ghisla, Sandro; Diekmann, Hans (Berlin : De Gruyter, 1999)

The proposed FAD binding site of L-lysine N6-hydroxylase (EC 1.14.13.99) exhibits an unusual proline in a position where a highly conserved glycine is found in other FAD dependent hydroxylases. We have studied the role of ...

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Auflistung nach Schlagwort "enzyme structure"

Auflistung nach Schlagwort "enzyme structure"

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