A Monte Carlo-based method to estimate radiation dose from spiral CT: from phantom testing to patient-specific models.

The purpose of this work is to develop and test a method to estimate the relative and absolute absorbed radiation dose from axial and spiral CT scans using a Monte Carlo approach. Initial testing was done in phantoms and preliminary results were obtained from a standard mathematical anthropomorphic model (MIRD V) and voxelized patient data. To accomplish this we have modified a general purpose Monte Carlo transport code (MCNP4B) to simulate the CT x-ray source and movement, and then to calculate absorbed radiation dose in desired objects. The movement of the source in either axial or spiral modes was modelled explicitly while the CT system components were modelled using published information about x-ray spectra as well as information provided by the manufacturer. Simulations were performed for single axial scans using the head and body computed tomography dose index (CTDI) polymethylmethacrylate phantoms at both central and peripheral positions for all available beam energies and slice thicknesses. For comparison, corresponding physical measurements of CTDI in phantom were made with an ion chamber. To obtain absolute dose values, simulations and measurements were performed in air at the scanner isocentre for each beam energy. To extend the verification, the CT scanner model was applied to the MIRD V model and compared with published results using similar technical factors. After verification of the model, the generalized source was simulated and applied to voxelized models of patient anatomy. The simulated and measured absolute dose data in phantom agreed to within 2% for the head phantom and within 4% for the body phantom at 120 and 140 kVp; this extends to 8% for the head and 9% for the body phantom across all available beam energies and positions. For the head phantom, the simulated and measured absolute dose data agree to within 2% across all slice thicknesses at 120 kVp. Our results in the MIRD phantom agree within 11% of all the different organ dose values published by the UK's ImPACT group for a scan using an equivalent scanner, kVp, collimation, pitch and mAs. The CT source model was shown to calculate both a relative and absolute radiation dose distribution throughout the entire volume in a patient-specific matrix geometry. Results of initial testing are promising and application to patient models was shown to be feasible.

Isolation and characterization of methanophenazine and function of phenazines in membrane-bound electron transport of Methanosarcina mazei Gö1.

A hydrophobic, redox-active component with a molecular mass of 538 Da was isolated from lyophilized membranes of Methanosarcina mazei Gö1 by extraction with isooctane. After purification on a high-performance liquid chromatography column, the chemical structure was analyzed by mass spectroscopy and nuclear magnetic resonance studies. The component was called methanophenazine and represents a 2-hydroxyphenazine derivative which is connected via an ether bridge to a polyisoprenoid side chain. Since methanophenazine was almost insoluble in aqueous buffers, water-soluble phenazine derivatives were tested for their ability to interact with membrane-bound enzymes involved in electron transport and energy conservation. The purified F42OH2 dehydrogenase from M. mazei Gö1 showed highest activity with 2-hydroxyphenazine and 2-bromophenazine as electron acceptors when F420H2 was added. Phenazine-1-carboxylic acid and phenazine proved to be less effective. The Km values for 2-hydroxyphenazine and phenazine were 35 and 250 microM, respectively. 2-Hydroxyphenazine was also reduced by molecular hydrogen catalyzed by an F420-nonreactive hydrogenase which is present in washed membrane preparations. Furthermore, the membrane-bound heterodisulfide reductase was able to use reduced 2-hydroxyphenazine as an electron donor for the reduction of CoB-S-S-CoM. Considering all these results, it is reasonable to assume that methanophenazine plays an important role in vivo in membrane-bound electron transport of M. mazei Gö1.