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Isonicotinium hydrogen sulfate.

ABSTRACT: The crystal structure of the title compound, C(6)H(6)NO(2) (+)·HSO(4) (-), is stabilized by inter-molecular N-H?O and O-H?O hydrogen bonds.

SUBMITTER: Chen LZ

PROVIDER: S-EPMC2970240 | biostudies-literature | 2009 Sep

REPOSITORIES: biostudies-literature

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Isonicotinium hydrogen sulfate.

Chen Li-Zhuang LZ

Acta crystallographica. Section E, Structure reports online 20090905 Pt 10

The crystal structure of the title compound, C(6)H(6)NO(2) (+)·HSO(4) (-), is stabilized by inter-molecular N-H⋯O and O-H⋯O hydrogen bonds. ...[more]

PMID: 21577818

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Anilinium hydrogen sulfate.

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Nicotinium hydrogen sulfate.

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Tris(4-hydroxy-pyridinium) hydrogen sulfate-sulfate monohydrate.

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4-Acetyl-pyridinium hydrogen sulfate.

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2-Amino-benzimidazolium hydrogen sulfate.

Project description:In the title salt, C(7)H(8)N(3) (+)·HSO(4) (-), the benzimdazole ring system is planar [mean deviation 0.0086?(1)?Å]. In the crystal, N-H?O and O-H?O hydrogen-bond inter-actions give rise to a layer motif.

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4-Hydroxy-pyridinium hydrogen sulfate.

Project description:The crystal structure of the title salt, C(5)H(6)NO(+)·HSO(4) (-), consists of planar(r.m.s. deviation = 0.001 Å) 4-hydroxy-pyridinium cations and hydrogen sulfate anions which are hydrogen bonded into a layer motif. In the anion, the S-O bond [1.551 (2) Å] involving the O atom bearing the acid H atom is longer than the other three S-O bonds, which range from 1.437 (1) to 1.454 (1) Å.

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4-Cyano-pyridinium hydrogen sulfate.

Project description:All non-H atoms of the cation of the title salt, C(6)H(5)N(2) (+)·HSO(4) (-), are essentially coplanar [r.m.s. deviation = 0.005 (1) Å] . In the crystal, N-H⋯O and O-H⋯O hydrogen bonds and weak C-H⋯O and C-H⋯N inter-actions link the mol-ecules into a two-dimensional network parallel to the (001) plane. Weak π-π stacking inter-actions between the pyridine rings of neighbouring mol-ecules further stabilize the structure [centroid-centroid distance = 3.785 (1) Å].

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2-Amino-pyrimidinium hydrogen sulfate.

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Hydrogen vs Lactate as electron donor in Sulfate reduction

Project description:In order to obtain a global view of energy metabolism pathways of the sulfate-reducer Desulfovibrio vulgaris Hildenborough and the proteins involved therein whole-genome microarrays were used to compare the transcriptional response of cells grown with hydrogen/sulfate, pyruvate/sulfate, lactate/thiosulfate, and pyruvate with limiting sulfate, relative to growth in standard lactate/sulfate condition. Growth with hydrogen/sulfate showed the largest number of differently expressed genes and the largest changes in expression levels. The most up-regulated energy metabolism genes were those coding for the periplasmic [NiFeSe] hydrogenase, followed by the Ech hydrogenase, and the most down-regulated were genes coding for the Coo hydrogenase. The results point to the involvement of formate cycling and the ethanol pathway during growth on hydrogen, whereas there is evidence for CO cycling during growth on lactate and pyruvate, but not on H2. Growth with thiosulfate showed the hallmarks of a reduced energy status of the cells with down regulation of the ATP synthase and the Qmo and Dsr complexes., whereas growth with pyruvate showed the smallest differences but an increased role for the Ech hydrogenase.that in this case functions in reverse from the case of growth with H2. The multiple periplasmic hydrogenases and formate dehydrogenases, do not display the same regulation pattern showing that their metabolic roles are not totally interchangeable. This result together with the observation that several genes coding for proteins that have not been biochemically characterised were considerably affected in this study, reveals a more complex energy metabolism than previously considered and provides guidance for further studies. Keywords: Growth protocol

2008-05-31 | GSE8037 | GEO

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