The study investigates the behavior of acidic MetMb and its higher oxidation state, confirming that two moles of H⁺ are released per mole of acidic MetMb. Using a pK of 6.1 for the group in MetMb, the results show a pK of 7.5 for the higher oxidation state at 20°C and I=0.04. The variation of K_obs with temperature gives ΔH°=10.0±2.0 kcal/mol, which is adjusted to 9.0±1.0 kcal/mol when considering ionization. The dependence of K_obs on ionic strength aligns with a charge change from +1 to 0. The results favor the ferryl ion structure for the higher oxidation state, with the higher oxidation state provisionally named ferrylmyoglobin. The study also examines the intracellular distribution of enzymes in rat liver tissue, revealing that several enzymes, including DPNH-cytochrome c reductase, TPNH-cytochrome c reductase, β-glucuronidase, cathepsin, ribonuclease, deoxyribonuclease, uricase, and fumarase, are associated with specific cytoplasmic granules. These granules have sedimentation properties between mitochondria and microsomes. The distribution of these enzymes is used as a reference framework for interpreting data on other enzymes. The results show that most enzymes are associated with one of three cytoplasmic particle groups: mitochondria, microsomes, or a special granule. The study confirms that cytochrome oxidase is associated with mitochondria, glucose-6-phosphatase with microsomes, and acid phosphatase with a special granule. The distribution of other enzymes is analyzed, showing that some follow the pattern of cytochrome oxidase, while others show complex distributions. The study also examines the activity of various enzymes, including acid phosphatase, β-glucuronidase, cathepsin, deoxyribonuclease, ribonuclease, glucose-6-phosphatase, and cytochrome c-linked enzymes. The results show that the activities of these enzymes are measured under specific conditions, with some enzymes showing a higher activity in the final supernatant. The study also explores the effects of various treatments on enzyme activity, including the use of Triton X-100, sucrose, and freezing/thawing. The results indicate that some enzymes are more active in the microsomal fraction, while others show a more uniform distribution. The study concludes that the distribution patterns of these enzymes reflect the presence of distinct systems in mitochondria and microsomes. The results also suggest that some enzymes may have a single intracellular location, while others may be distributed unevenly between microsomes and the final supernatant. The study highlights the importance of these findings inThe study investigates the behavior of acidic MetMb and its higher oxidation state, confirming that two moles of H⁺ are released per mole of acidic MetMb. Using a pK of 6.1 for the group in MetMb, the results show a pK of 7.5 for the higher oxidation state at 20°C and I=0.04. The variation of K_obs with temperature gives ΔH°=10.0±2.0 kcal/mol, which is adjusted to 9.0±1.0 kcal/mol when considering ionization. The dependence of K_obs on ionic strength aligns with a charge change from +1 to 0. The results favor the ferryl ion structure for the higher oxidation state, with the higher oxidation state provisionally named ferrylmyoglobin. The study also examines the intracellular distribution of enzymes in rat liver tissue, revealing that several enzymes, including DPNH-cytochrome c reductase, TPNH-cytochrome c reductase, β-glucuronidase, cathepsin, ribonuclease, deoxyribonuclease, uricase, and fumarase, are associated with specific cytoplasmic granules. These granules have sedimentation properties between mitochondria and microsomes. The distribution of these enzymes is used as a reference framework for interpreting data on other enzymes. The results show that most enzymes are associated with one of three cytoplasmic particle groups: mitochondria, microsomes, or a special granule. The study confirms that cytochrome oxidase is associated with mitochondria, glucose-6-phosphatase with microsomes, and acid phosphatase with a special granule. The distribution of other enzymes is analyzed, showing that some follow the pattern of cytochrome oxidase, while others show complex distributions. The study also examines the activity of various enzymes, including acid phosphatase, β-glucuronidase, cathepsin, deoxyribonuclease, ribonuclease, glucose-6-phosphatase, and cytochrome c-linked enzymes. The results show that the activities of these enzymes are measured under specific conditions, with some enzymes showing a higher activity in the final supernatant. The study also explores the effects of various treatments on enzyme activity, including the use of Triton X-100, sucrose, and freezing/thawing. The results indicate that some enzymes are more active in the microsomal fraction, while others show a more uniform distribution. The study concludes that the distribution patterns of these enzymes reflect the presence of distinct systems in mitochondria and microsomes. The results also suggest that some enzymes may have a single intracellular location, while others may be distributed unevenly between microsomes and the final supernatant. The study highlights the importance of these findings in