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Alexander J. B. Zehnder

Researcher at Swiss Federal Institute of Aquatic Science and Technology

Publications -  188
Citations -  24992

Alexander J. B. Zehnder is an academic researcher from Swiss Federal Institute of Aquatic Science and Technology. The author has contributed to research in topics: Polyphosphate & Phosphate. The author has an hindex of 78, co-authored 188 publications receiving 23933 citations. Previous affiliations of Alexander J. B. Zehnder include École Polytechnique Fédérale de Lausanne & ETH Zurich.

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Factors affecting mass transfer limited biodegradation in saturated porous media.

TL;DR: Mass transfer limitation offers a justification for the common assumption that biodegradation rates in the subsurface follow first order kinetics in a wide concentration range.
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Ferrous iron dependent nitric oxide production in nitrate reducing cultures of Escherichia coli

TL;DR: Ferric iron reduction activity in E. coli E4 was found to be constitutive and ferric iron could not be used as electron acceptor for growth, unlike nitrate, which was anaerobically converted to nitric oxide and nitrous oxide.
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Characterization of two phosphate transport systems in Acinetobacter johnsonii 210A.

TL;DR: Results suggest that the high-affinity transport system belongs to the group of ATP-driven, binding-protein-dependent transport systems, and the ability to decrease the free internal P(i) pool by forming polyP enable A. johnsonii 210A to reduce the P( i) concentration in the aerobic environment to micromolar levels.
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Polysaccharide synthesis in relation to nodulation behavior of Rhizobium leguminosarum

TL;DR: It is impossible to correlate a defect in the synthesis of a particular polysaccharide with nodulation characteristics, so it is hypothesize that this strain RBL5515 exo-344::Tn5 is affected in a galactose transferase involved inThe synthesis of EPS only.
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Enzymatic evidence for involvement of the methylmalonyl-CoA pathway in propionate oxidation by Syntrophobacter wolinii.

TL;DR: Most of the enzymes involved in the methylmalonyl- CoA pathway for propionate oxidation, including a propionyl-CoA: oxaloacetate transcarboxylase, were demonstrated in S. wolinii.