• Publications
  • Influence
Choline monooxygenase, an unusual iron-sulfur enzyme catalyzing the first step of glycine betaine synthesis in plants: prosthetic group characterization and cDNA cloning.
RNA and immunoblot analyses showed that the expression of CMO in leaves increased several-fold during salinization, concluding that CMO is a stress-inducible representative of a new class of plant oxygenases. Expand
Shewanella oneidensis MR-1 nanowires are outer membrane and periplasmic extensions of the extracellular electron transport components
Using in vivo fluorescence measurements, immunolabeling, and quantitative gene expression analysis, it is demonstrated that S. oneidensis MR-1 nanowires are extensions of the outer membrane and periplasm that include the multiheme cytochromes responsible for EET, rather than pilin-based structures as previously thought. Expand
PsaE Is Required for in Vivo Cyclic Electron Flow around Photosystem I in the Cyanobacterium Synechococcus sp. PCC 7002
It is concluded that, although PsaE is not required for linear electron flow to NADP+, it is an essential component in the cyclic electron transport pathway around photosystem I and there are three major electron sources for P700+ reduction in this cyanobacteria. Expand
The sufR Gene (sll0088 in Synechocystis sp. Strain PCC 6803) Functions as a Repressor of the sufBCDS Operon in Iron-Sulfur Cluster Biogenesis in Cyanobacteria
It is proposed that the protein encoded by sll0088 is a transcriptional repressor of the suf operon, and the gene sufR is named, in agreement with the proposed role of thesufBCDS genes in iron metabolism. Expand
INTRODUCTION . . . . . ........ . . . . . . .. . . . . . . . . . . . . . . . . . . . .. . . . .. . . . . . .. . ..... ...... . . . . . . . .. . . . . . . . . . . 293 PHOTOSYSTEM I REACTION CENTER . .Expand
Cloning and characterization of the psaE gene of the cyanobacterium Synechococcus sp. PCC 7002: characterization of a psaE mutant and overproduction of the protein in Escherichia coli
The psaE gene, encoding a 7.5 kDa peripheral protein of the photosystem I complex, has been cloned and characterized from the cyanobacterium Synechococcus sp. PCC 7002. The gene is transcribed as anExpand
Regulatory Roles for IscA and SufA in Iron Homeostasis and Redox Stress Responses in the Cyanobacterium Synechococcus sp. Strain PCC 7002
The growth phenotypes and mRNA abundance patterns of the mutant strains contradict the proposed scaffold function for the SufA and IscA proteins in generalized Fe/S cluster assembly and instead suggest that they play regulatory roles in iron homeostasis and the sensing of redox stress in cyanobacteria. Expand
PsaD is required for the stable binding of PsaC to the photosystem I core protein of Synechococcus sp. PCC 6301.
The data indicate that although PsaC can bind loosely, the presence of PsaD leads to a stable, isolatable photosystem I complex which is spectroscopically indistinguishable from the native complex. Expand
Recruitment of a foreign quinone into the A(1) site of photosystem I. I. Genetic and physiological characterization of phylloquinone biosynthetic pathway mutants in Synechocystis sp. pcc 6803.
Targeted inactivation of the menA and menB genes, which code for phytyl transferase and 1,4-dihydroxy-2-naphthoate synthase prevented the synthesis of phylloquinone, thereby confirming the participation of these two gene products in the biosynthetic pathway. Expand
Protein-cofactor interactions in bioenergetic complexes: the role of the A1A and A1B phylloquinones in Photosystem I.
This review focuses on phylloquinone as an indispensable link between light-induced charge separation and subsequent charge stabilization in Photosystem I (PS I), with particular emphasis on the determination of redox potentials of the cofactors. Expand