[Fe2{SeC6H2‐2,4,6‐Ph3}2{N(SiMe3)2}2] and [Fe2{SeC6H2‐2,4,6‐Ph3}4], the First Three‐Coordinate Selenolatoiron Complexes

In a controlled manner , half or all the bis(trimethylsilyl)amido ligands of 1 can be replaced by selenolato ligands, resulting in the first selenolatoiron complexes 2 and 3 with three‐coordinate iron centers. They are stabilized by secondary metal–framework bonds (here metal–carbon) and could, since they are coordinatively unsaturated, possibly serve as model compounds of the FeMo cofactor of nitrogenases.     

优化固氮活性模型信息研究—双齿配体DPPE和DPPM对固氮酶促反应的影响

报道了某些双齿配体对固氮酶促反应影响的研究结果．发现１，２－双（二苯基磷）－乙烷（ＤＰＰＥ）对固氮酶酶促乙炔还原反应有促进作用，但同时又抑制了固氮酶的放氢反应。而比ＤＰＰＥ少一个－ＣＨ２－链的双（二苯基磷）－甲烷（ＤＰＰＭ）却不能表现出对固氮酶促乙炔还原活力的促进作用．对照固氮酶ＭｏＦｅ－蛋白Ｘ－光衍射结构分析结果和量子化学近似计算所导出的固氮酶活性中心结构模型提出了ＤＰＰＥ促进酶促乙炔还原反应的一种可能的解释．     

Characterization of nitrogen-fixing moderate halophilic cyanobacteria isolated from saline soils of Songnen Plain in China

Twenty out of 200 isolates of cyanobacteria mainly from saline soils of Songnen Plain of China were successfully grown on BG11 N-free medium. The nitrogen-fixing activity was then demonstrated for the twenty isolates in modified BG11 medium using the acetylene reduction assay. All of them possessed appreciable nitrogenase activity (acetylene reduction) under non-saline conditions; however, at 5 % NaCl only 60 % of the isolates exhibited a high rate of this activity and 25 % were completely negative under these conditions. The cyanobacteria isolates grew well in BG11 medium; nevertheless, growth of the majority of isolates was reduced by about 25%-85% in the same medium containing 5% NaCl. Cellulolytic activity was detected in 50% of the twenty strains, amylolytic in 45%, and pectinolytic in 10% of the isolates. The cyanobacteria isolates showed also enzymeatic activity under saline conditions (6%). The preliminary identification indicated that seven isolates were Nostoc, two were Microcystis, four were Oscillatoria, six were Anabaena, and one isolate was Synechococcus.      

Bioelectrochemical Haber–Bosch Process: An Ammonia‐Producing H2/N2 Fuel Cell

Nitrogenases are the only enzymes known to reduce molecular nitrogen (N₂) to ammonia (NH₃). By using methyl viologen (N ,N ′‐dimethyl‐4,4′‐bipyridinium) to shuttle electrons to nitrogenase, N₂ reduction to NH₃ can be mediated at an electrode surface. The coupling of this nitrogenase cathode with a bioanode that utilizes the enzyme hydrogenase to oxidize molecular hydrogen (H₂) results in an enzymatic fuel cell (EFC) that is able to produce NH₃ from H₂ and N₂ while simultaneously producing an electrical current. To demonstrate this, a charge of 60 mC was passed across H₂ /N₂ EFCs, which resulted in the formation of 286 nmol NH₃ mg⁻¹ MoFe protein, corresponding to a Faradaic efficiency of 26.4 %.     

X‐ray Magnetic Circular Dichroism Spectroscopy Applied to Nitrogenase and Related Models: Experimental Evidence for a Spin‐Coupled Molybdenum(III) Center

Nitrogenase enzymes catalyze the reduction of atmospheric dinitrogen to ammonia utilizing a Mo‐7Fe‐9S‐C active site, the so‐called FeMoco cluster. FeMoco and an analogous small‐molecule (Et₄N)[(Tp)MoFe₃S₄Cl₃] cubane have both been proposed to contain unusual spin‐coupled Mo^III sites with an S(Mo)=1/2 non‐Hund configuration at the Mo atom. Herein, we present Fe and Mo L₃‐edge X‐ray magnetic circular dichroism (XMCD) spectroscopy of the (Et₄N)[(Tp)MoFe₃S₄Cl₃] cubane and Fe L_2,3‐edge XMCD spectroscopy of the MoFe protein (containing both FeMoco and the 8Fe‐7S P‐cluster active sites). As the P‐clusters of MoFe protein have an S=0 total spin, these are effectively XMCD‐silent at low temperature and high magnetic field, allowing for FeMoco to be selectively probed by Fe L_2,3‐edge XMCD within the intact MoFe protein. Further, Mo L₃‐edge XMCD spectroscopy of the cubane model has provided experimental support for a local S(Mo)=1/2 configuration, demonstrating the power and selectivity of XMCD.     

On the structure-function relationship of nitrogenase M-cluster and P-cluster pairs

It A proposed that the M-cluster cage (Kim-Rees model) in active N₂-ase can exert shape-selective molecular-sieve effects in molecular recognition of exogenous substrates, by providing inside multinuclear active-sites the cavity for N₂, C₂H₂, cyclopropene, and N₂O reduction, with [Mo-3Fe]-site available only for N₂ reduction: on the other handn-RC— CH,n-RC— N,n-RN-C , C—N^– and N₃ ^–, are bound outside the cavity at the [2Fe]-site left by the labilizable ligand Y. A terminal carboxylate of the Mo-bound (R)-homocitrate is just in position to protect a H₂-evolution site on the P-cluster pair from CO inhibition, and also to take part in mediating a P-cluster-to-Mo-site H⁺-relay system (involving two hydrogen-bonded H₂O) specifically required for N. reduction. The nonreducibility of CO at the [Mo-3Fe]-site is also explained. Experimental support for molecular-sieve effects of M-cluster cage has been obtained from the observed decrease in ethene-cis-d: selectivity by competitive inhibition of HC—CH reduction in D₂O by N—N.Dedicated to Jiaxi Lu on the occasion of his 80th birthday.     

Nonenzymatic Simulation of Nitrogenase Reactions and the Mechanism of Biological Nitrogen Fixation

The development of biologically relevant model systems of nitrogenase permitted the simulation of virtually all known reactions of the nitrogen reducing enzymes under nonenzymatic conditions. On the basis of these experiments, a mechanism of biological nitrogen fixation is formulated which is in accord with the available enzymological evidence. The key reactions of the substrates of nitrogenase occur at a molybdenum active site. The non-heme iron, which is bound to sulfur and protein-S^? groups, mediates the transport of electrons to the molybdenum active site but does not participate directly in the reduction of the substrates. ATP is required for the acceleration of the reduction and activation of the molybdenum site and is hydrolyzed to ADP and inorganic phosphate. Diimine and hydrazine were detected as intermediates in the reduction of molecular nitrogen under nonenzymatic conditions.     

含质子柠檬酸氧钒（V）配合物中间体的合成和晶体结构

合成了含质子柠檬酸氧钒（Ｖ）配合物中间体ＮａＫ３［ＶＯ２（Ｈｃｉｔ）］２·７Ｈ２Ｏ，用红外光谱和Ｘ射线衍射进行了结构表征。结果表明：晶体属单斜晶系，Ｐ２１／ｎ空间群。晶胞参数ａ＝１．１２５８（２）ｎｍ，ｂ＝１．５７７４（３）ｎｍ，ｃ＝１６５５９（１）ｎｍ，β＝９８．５６８（９）°，Ｖ＝２．９０８（１）ｎｍ＾３，Ｚ＝４，Ｄｃ＝１．８５１ｇ·ｃｍ＾－３，Ｆ（０００）＝１６４０，μ（Ｃｕ Ｋα）＝１０４