Asymmetric Phosphorus Incorporation in Homoepitaxial P-Doped (111) Diamond Revealed by Photoelectron Holography.

Diamond has two crystallographically inequivalent sites in the unit cell. In doped diamond, dopant occupation in the two sites is expected to be equal. Nevertheless, preferential dopant occupation during growth under nonequilibrium conditions is of fundamental importance, for example, to enhance the properties of nitrogen-vacancy (N-V) centers; therefore, this is a promising candidate for a qubit. However, the lack of suitable experimental techniques has made it difficult to study the crystal- and chemical-site-resolved local structures of dopants. Here, we confirm the identity of two chemical sites with asymmetric dopant incorporation in the diamond structure, via the photoelectron holography (PEH) of heavily phosphorus (P)-doped diamond prepared by chemical vapor deposition. One is substitutionally incorporated P with preferential site occupations and the other can be attributed to a PV split vacancy complex with preferential orientation. The present study shows that PEH is a valuable technique to study the local structures around dopants with a resolution of crystallographically inequivalent but energetically equivalent sites/orientations. Such information provides strategies to improve the properties of dopant related-complexes in which alignment is crucial for sensing of magnetic field or quantum spin register using N-V centers in diamond.

Cloning, overexpression, and mutagenesis of the Sporobolomyces salmonicolor AKU4429 gene encoding a new aldehyde reductase, which catalyzes the stereoselective reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (S)-4-chloro-3-hydroxybutanoate.

We cloned and sequenced the gene encoding an NADPH-dependent aldehyde reductase (ARII) in Sporobolomyces salmonicolor AKU4429, which reduces ethyl 4-chloro-3-oxobutanoate (4-COBE) to ethyl (S)-4-chloro-3-hydroxybutanoate. The ARII gene is 1,032 bp long, is interrupted by four introns, and encodes a 37,315-Da polypeptide. The deduced amino acid sequence exhibited significant levels of similarity to the amino acid sequences of members of the mammalian 3beta-hydroxysteroid dehydrogenase-plant dihydroflavonol 4-reductase superfamily but not to the amino acid sequences of members of the aldo-keto reductase superfamily or to the amino acid sequence of an aldehyde reductase previously isolated from the same organism (K. Kita, K. Matsuzaki, T. Hashimoto, H. Yanase, N. Kato, M. C.-M. Chung, M. Kataoka, and S. Shimizu, Appl. Environ. Microbiol. 62:2303-2310, 1996). The ARII protein was overproduced in Escherichia coli about 2, 000-fold compared to the production in the original yeast cells. The enzyme expressed in E. coli was purified to homogeneity and had the same catalytic properties as ARII purified from S. salmonicolor. To examine the contribution of the dinucleotide-binding motif G(19)-X-X-G(22)-X-X-A(25), which is located in the N-terminal region, during ARII catalysis, we replaced three amino acid residues in the motif and purified the resulting mutant enzymes. Substrate inhibition of the G(19)-->A and G(22)-->A mutant enzymes by 4-COBE did not occur. The A(25)-->G mutant enzyme could reduce 4-COBE when NADPH was replaced by an equimolar concentration of NADH.