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Isopentenyl phosphate kinases (IPKs) have recently garnered attention for their central role in biocatalytic "isoprenol pathways," which seek to reduce the synthesis of the isoprenoid precursors to two enzymatic steps. Furthermore, the natural promiscuity of IPKs toward non‐natural alkyl‐monophosphates (alkyl‐Ps) as substrates has hinted at the isoprenol pathways' potential to access novel isoprenoids with potentially useful activities. However, only a handful of IPK crystal structures have been solved to date, and even fewer of these contain non‐natural substrates bound in the active site. The current study sought to elucidate additional ternary complexes bound to non‐natural substrates using the IPK homolog from Thermococcus paralvinellae (TcpIPK). Four such structures were solved, each bound to a different non‐natural alkyl‐P and the phosphoryl donor substrate/product adenosine triphosphate (ATP)/adenosine diphosphate (ADP). As expected, the quaternary, tertiary, and secondary structures of TcpIPK closely resembled those of IPKs published previously, and kinetic analysis of a novel alkyl‐P substrate highlighted the potentially dramatic effects of altering the core scaffold of the natural substrate. Even more interesting, though, was the discovery of a trend correlating the position of two α helices in the active site with the magnitude of an IPK homolog's reaction rate for the natural reaction. Overall, the current structures of TcpIPK highlight the importance of continued structural analysis of the IPKs to better understand and optimize their activity with both natural and non‐natural substrates. [ABSTRACT FROM AUTHOR]

Basicities of metal within mononuclear organometallic compounds act as indictors of other reactivities. The basicities of the metal-metal bonds in a set of Cp'sub2Rusub2(CO)sub4 compounds containing several cyclopentadienyl-type ligands, are reported, using titration calorimetry. They are defined as the enthalpies of protonation (DeltaHMHM) of metal compounds with triflic acid (CFsub3SOsub3H) with 1,2-dichlorethane solution.

The complex [trans-(Cl)([14]aneN4)RhH}2(ZnCl4).dmso exhibited a spectral resonance of 1530 centimeters-1 during spectroscopic analysis due to the presence of a Rh-D stretch. The hydride resonances of the cis- and trans-(Cl)L1RhH2+ are characteristic frequencies of isomers. The macrocyclic rhodium hydride is composed of asymmetric units that is made up of two rhodium cations, a tetrachlorozincate anion and a molecule of dmso. The hydride ligand or hydridorhodium(III) complex forms a pseudooctahedral geometry around the rhodium by occupying the axial position of the chloride.

Heme is an important cofactor in a large number of essential proteins and is often involved in small molecule binding and activation. Loss of heme from proteins thus negatively affects the function of these proteins but is also an important component of iron recycling. The characterization of intermediates that form during the loss of heme from proteins has been problematic, in a large part, because of the instability of such intermediates. We have characterized, by X-ray crystallography, three compounds that form during the nitrite-induced degradation of human α2β2 hemoglobin (Hb). The first is an unprecedented complex that exhibits a large β heme displacement of 4.8 Å toward the protein exterior; the heme displacement is stabilized by the binding of the distal His residue to the heme Fe, which in turn allows for the unusual binding of an exogenous ligand on the proximal face of the heme. We have also structurally characterized complexes that display regiospecific nitration of the heme at the 2-vinyl position; we show that heme nitration is not a prerequisite for heme loss. Our results provide structural insight into a possible pathway for nitrite-induced loss of heme from human Hb. [ABSTRACT FROM AUTHOR]

The crystal structure of AdhP, a recombinantly expressed alcohol dehydrogenase from Escherichia coli K-12 (substrain MG1655), was determined to 2.01 Å resolution. The structure, which was solved using molecular replacement, also included the structural and catalytic zinc ions and the cofactor nicotinamide adenine dinucleotide (NAD). The crystals belonged to space group P21, with unit-cell parameters a = 68.18, b = 118.92, c = 97.87 Å, β = 106.41°. The final R factor and Rfree were 0.138 and 0.184, respectively. The structure of the active site of AdhP suggested a number of residues that may participate in a proton relay, and the overall structure of AdhP, including the coordination to structural and active-site zinc ions, is similar to those of other tetrameric alcohol dehydrogenase enzymes. [ABSTRACT FROM AUTHOR]