No abstract

Methyl iodide (CH(3)I) plays an important role in the natural iodine cycle and participates in atmospheric ozone destruction. However, the main source of this compound in nature is still unclear. Here we report that a wide variety of bacteria including terrestrial and marine bacteria are capable of methylating the environmental level of iodide (0.1 microM). Of the strains tested, Rhizobium sp. strain MRCD 19 was chosen for further analysis, and it was found that the cell extract catalyzed the methylation of iodide with S-adenosyl-L-methionine as the methyl donor. These results strongly indicate that bacteria contribute to iodine transfer from the terrestrial and marine ecosystems into the atmosphere.

Iodide-oxidizing bacteria (IOB), which oxidize iodide (I-) to molecular iodine (I2), were isolated from iodide-rich (63 microM to 1.2 mM) natural gas brine waters collected from several locations. Agar media containing iodide and starch were prepared, and brine waters were spread directly on the media. The IOB, which appeared as purple colonies, were obtained from 28 of the 44 brine waters. The population sizes of IOB in the brines were 10(2) to 10(5) colony-forming units (CFU) mL(-1). However, IOB were not detected in natural seawaters and terrestrial soils (fewer than 10 CFU mL(-1) and 10(2) CFU g wet weight of soils(-1), respectively). Interestingly, after the enrichment with 1 mM iodide, IOB were found in 6 of the 8 seawaters with population sizes of 10(3) to 10(5) CFU mL(-1). 16S rDNA sequencing and phylogenetic analyses showed that the IOB strains are divided into two groups within the alpha-subclass of the Proteobacteria. One of the groups was phylogenetically most closely related to Roseovarius tolerans with sequence similarities between 94% and 98%. The other group was most closely related to Rhodothalassium salexigens, although the sequence similarities were relatively low (89% to 91%). The iodide-oxidizing reaction by IOB was mediated by an extracellular enzyme protein that requires oxygen. Radiotracer experiments showed that IOB produce not only I2 but also volatile organic iodine, which were identified as diiodomethane (CH2I2) and chloroiodomethane (CH2ClI). These results indicate that at least two types of IOB are distributed in the environment, and that they are preferentially isolated in environments in which iodide levels are very high. It is possible that IOB oxidize iodide in the natural environment, and they could significantly contribute to the biogeochemical cycling of iodine.

Iodine is an essential trace element for humans and animals because of its important role as a constituent of thyroid hormones. If the anthropogenic iodine-129 ( 129 I, half-life: 1.6×10 7 years), which is released from nuclear facilities into the environment and has a long half-life, participates in the biogeochemical cycling of iodine, it potentially accumulates in the human thyroid gland and might cause thyroid cancer. Therefore, it is necessary to obtain better information on the behavior of iodine in the environment for accurate safety assessments of 129 I. Major pathways of iodine cycling are the volatilization of organic iodine compounds into the atmosphere, accumulation of iodine in living organisms, oxidation and reduction of inorganic iodine species, and sorption of iodine by soils and sediments. Considerable geochemical evidence has indicated that these processes are influenced or controlled by microbial activities, although the precise mechanisms involved are still unclear. This review summarizes current knowledge on interactions between microorganisms and iodine, with special emphasis on newly isolated bacteria possibly contributing to the cycling of iodine on a global scale.

Pseudomonas sp. strain SCT is capable of using iodate (IO 3 − ) as a terminal electron acceptor for anaerobic respiration. A possible key enzyme, periplasmic iodate reductase (Idr), was visualized by active staining on non-denaturing gel electrophoresis. Liquid chromatography-tandem mass spectrometry analysis revealed that at least four proteins, designated as IdrA, IdrB, IdrP 1 , and IdrP 2 , were involved in Idr. IdrA and IdrB were homologues of catalytic and electron transfer subunits of respiratory arsenite oxidase (Aio); however, IdrA defined a novel clade within the dimethylsulfoxide (DMSO) reductase family. IdrP 1 and IdrP 2 were closely related to each other and distantly related to cytochrome c peroxidase. The idr genes (idrABP 1 P 2 ) formed an operon-like structure, and their transcription was upregulated under iodate-respiring conditions. Comparative proteomic analysis also revealed that Idr proteins and high affinity terminal oxidases (Cbb 3 and Cyd), various H 2 O 2 scavengers, and chlorite (ClO 2 − ) dismutase-like proteins were expressed specifically or abundantly under iodate-respiring conditions. These results suggest that Idr is a respiratory iodate reductase, and that both O 2 and H 2 O 2 are formed as by-products of iodate respiration. We propose an electron transport chain model of strain SCT, in which iodate, H 2 O 2 , and O 2 are used as terminal electron acceptors.