ChemInform Abstract: Phosphine Binding as a Structural Probe of the Chloroperoxidase Active Sitc: Spectroscopic Evidence for Endogenous Thiolate Ligation to the Heme Iron

This study was undertaken to estimate the contribution of meat and meat products consumption to the daily intakes of trace elements (Fe, Zn, Cu, Se), heme iron, and selected B vitamins (thiamine, riboflavin, niacin) in Italy. Meat and meat products were selected on the basis of their consumption frequency reported by the most recent nationwide dietary individual survey carried out in Italy (INN-CA study). The daily intakes of total iron and heme iron were 1.65 and 1.13 mg/person/day. Zinc intake was 3.65 mg/person/day. Beef made the main contribution to iron, heme iron, and zinc daily intakes. Copper daily intake was 107.3 mug/person/day, with meat products provided the highest contribution (40 mug/person/day). Daily intake of selenium (7.14 mug/person/day) was provided mainly by poultry consumption. Thiamine intake was 228 mug/person/day, and meat products were the main source (110 mug/person/day). Riboflavin intake was 136 mug/person/day, with both beef and meat products as the main contributors (40 mug/person/day). Niacin intake was 7.53 mg/person/day, and poultry was the main source (2.28 mg/person/day). Meat and meat products were a valuable source of micronutrients, supplying 47, 48, and 24% of zinc, niacin, and thiamin daily requirements, respectively, and over 10% of iron, copper, selenium, and riboflavin daily average requirement values of the italian RDAs calculated for the population involved in the survey (INN-CA study).

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NADH in Solution: A Single State

10.26434/chemrxiv.8208407.v1 ◽

2019 ◽

Author(s):

Joachim Hönes ◽

Julia Wack ◽

Katja Schmitz

Keyword(s):

Aqueous Solution ◽

Base Stacking ◽

Spectroscopic Evidence ◽

Single State

<div>Spectroscopic evidence is presented to show that NADH in aqueous solution does not exist as a folded/unfolded equilibrium but as a single state. The molecule is folded but without base stacking between dihydronicotinamide and adenine.<br></div>

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Strongly Coupled Redox-Linked Conformational Switching at the Active Site of the Non-Heme Iron-Dependent Dioxygenase, TauD

10.26434/chemrxiv.9461462 ◽

2019 ◽

Author(s):

Christopher John ◽

Greg M. Swain ◽

Robert P. Hausinger ◽

Denis A. Proshlyakov

Keyword(s):

Active Site ◽

Structural Model ◽

Heme Iron ◽

Chemical Transformations ◽

Experimental Conditions ◽

Strongly Coupled ◽

Non Heme Iron ◽

Reversible Redox ◽

Wide Range ◽

Complex Structural

2-Oxoglutarate (2OG)-dependent dioxygenases catalyze C-H activation while performing a wide range of chemical transformations. In contrast to their heme analogues, non-heme iron centers afford greater structural flexibility with important implications for their diverse catalytic mechanisms. We characterize an <i>in situ</i> structural model of the putative transient ferric intermediate of 2OG:taurine dioxygenase (TauD) by using a combination of spectroelectrochemical and semi-empirical computational methods, demonstrating that the Fe (III/II) transition involves a substantial, fully reversible, redox-linked conformational change at the active site. This rearrangement alters the apparent redox potential of the active site between -127 mV for reduction of the ferric state and 171 mV for oxidation of the ferrous state of the 2OG-Fe-TauD complex. Structural perturbations exhibit limited sensitivity to mediator concentrations and potential pulse duration. Similar changes were observed in the Fe-TauD and taurine-2OG-Fe-TauD complexes, thus attributing the reorganization to the protein moiety rather than the cosubstrates. Redox difference infrared spectra indicate a reorganization of the protein backbone in addition to the involvement of carboxylate and histidine ligands. Quantitative modeling of the transient redox response using two alternative reaction schemes across a variety of experimental conditions strongly supports the proposal for intrinsic protein reorganization as the origin of the experimental observations.

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